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POPROTEIN!ClilmalateR6 TTUREe7 l6 lye6 e52embraneilatilatoodassp60i immunizationaoncubatedn ion0 s s s  s  sigmullersnerK  l K KC KALLIKREINl%liminaryI m| m m  m X m  m m m m m 4 M! m P! POPROTEINmalateTUREtilattW%&&%%Geb&/+*"'j -{-t-+I' (--(t^u^(nl@4P&!"#y(@&(A%+!z -Q%r+,!X$)%=,wI5&%h~mI~~V(qbJ(Gm+ !!#+!3""xo$+(^E $<(sR0_~ _;U$!)Z!;_ %)-t&"*g)Z,,,,,,""""}$@k'$!U*r z z zeeeeeeeeee!+++,,,,$$$$$$$$",f,f,f,f&&&&&&000000FFFFFFFF!!!!!!!!!! !               %%%%%%%"f"f"f"f"f"f"f"f,,,,,,,$$$$$$........../B9D@ 148"Andersson, H. Vonheijne, G.a 1993CYTOPLASMIC MEMBRANE ESCHERICHIA-COLI EXPORT HYDROPHOBIC DOMAIN INSERTION LEADER PEPTIDASE M13 PROCOAT PROTEIN MEMBRANE-PROTEIN PLASMA-MEMBRANE POSITIVELY CHARGED RESIDUES PROTEIN SECRETION TOPOLOGY TRANSLOCATIONrlTranslocation of proteins across the inner membrane of Escherichia coli normally requires the participation of the sec machinery. A number of proteins are known, however, where translocation can proceed unhindered even when the function of either SecA or SecY, central components of the sec machinery, is blocked. We now show that there is a linear correlation between the length of a translocated region and its degree of dependence on SecA and SecY for lengths between 25 and 55 residues. We also find that positively charged residues have distinctly different topological effects during SecA dependent and SecA independent membrane protein insertion, and that a short cytoplasmic segment in Lep can be converted to a translocated segment (with a concomitant inversion of the original topology of the whole molecule) by increasing its length into the SecA/Y dependent realm.{Sec Dependent and sec Independent Assembly of E-Coli Inner Membrane Proteins - The Topological Rules Depend on Chain Lengthe EMBO Journal122683-691. Feb8"Andersson, H. Vonheijne, G.d 1994{Membrane protein topology: effects of mu H+ on the translocation of charged residues explain the 'positive inside' rule. EMBO Journal1310 2267-2272 b[The membrane electrochemical potential is critical for the export of most periplasmic proteins in Escherichia coli. Its exact role during insertion of integral inner membrane proteins, however, remains obscure. Using derivatives of the inner membrane protein leader peptidase (Lep), we now show that the membrane potential appears to stimulate the membrane translocation of chain segments containing negatively charged residues, that positively charged regions appear to be more easily translocated in the absence of a potential, and that certain Lep constructs insert with different topologies in the presence and absence of a membrane potential, suggesting that the electrochemical potential introduces an asymmetry between the topological effects of positively and negatively charged amino acids during the process of membrane protein insertion in E. coli."Andersson, H. Vonheijne, G. 1994Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane. FEBS Letters 347u169-172The sec machinery catalyzes the translocation of nascent polypeptide chains across the inner membrane of E. coli, yet some inner membrane proteins depend only weakly or not at all on an intact sec function for membrane insertion even though they have stretches of chain protruding into the periplasmic space. Earlier work has demonstrated that the length of a periplasmic loop correlates with its degree of sec-dependence. We now show that the content of positively charged residues in a translocated loop also correlates with the degree of dependence on SecA function, suggesting that arginines and lysines may be inherently difficult to move across the membrane during sec-dependent translocation.Andersson, D.I. 20032+Pesistence of antibiotic resistant bacteriaCurr Opin Microbiol 6452-456 KSR& Ando, T. Yamasaki, M. Suzuki, K. 1973F@Protamines: isolation, characterization, structure and function4.Molecular Biology, Biochemistry and Biophysics New York Springer12 150@9Ando, S. Nishikawa, H. Takiguchi, H. Lee, S. Sugihara, G. 1993AMPHIPHILIC BETA-STRUCTURAL PEPTIDE ANALOGS ANTIBACTERIAL PEPTIDES ANTIMICROBIAL ACTIVITY CD CONFORMATIONS GRAMICIDIN-S HEMOLYSIS LIPOSOME MEMBRANES NEUTROPHILS PEPTIDE PHOSPHOLIPID PEPTIDE INTERACTIONgAntimicrobial Specificity and Hemolytic Activity of Cyclized Basic Amphiphilic beta-Structural Model Peptides and Their Interactions with Phospholipid Bilayers $Biochimica et Biophysica Acta  11471t 42-49 8 Apr$ EmbOE$3r$r$r*r$r%r*-r'%r+Ur+Vr+Wr+]r+r+fr*rr)Dr+pr+r+r+r+r(rr,lr,r,r,r,r,rr)r-^rhr-|r.r*rr0Er0r0r0r0r0r0r0r0r0r0r1r)/r&r0r0r)Mr1r1Wr1Xr1Yr1ur1}r1}r22.P/2*22122>22D22T22Z22Y22[22\22]22022p22w2222222222222222222222222221j222222222222222222222222222 t2222222222222222222222232323 23 232323232323QUery3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s3s Nishikawa, H. Takiguchi, H. Lee, S. Sugihara, G. 1993AMPHIPHILIC BETA-STRUCTURAL PEPTIDE ANALOGS ANTIBACTERIAL PEPTIDES ANTIMICROBIAL ACTIVITY CD CONFORMATIONS GRAMICIDIN-S HEMOLYSIS LIPOSOME MEMBRANES NEUTROPHILS PEPTIDE PHOSPHOLIPID PEPTIDE INTERACTIONgAntimicrobial Specificity and Hemolytic Activity of Cyclized Basic Amphiphilic beta-Structural Model Peptides and Their Interactions with Phospholipid Bilayers $Biochimica et Biophysica Acta  11471t 42-49 8 Aprdddd$$$$#y#y#y#y#y00-bx#d#d#d#d#d#d#d#d#d#d#d&-&-&-&->}+,}-H- G! $U>i%&*W:::''''''''''''BBB222222222""AAAAA%%%A%%%%+\+\+\+\+\+\+\+\+\+\33333,,,,,,,,22+22++++###)))$JJJJJJ$J$$$$$$$$44444KKKKKKKKKKKKKKKGGGGGGGGGGGGGGGHHHHHH&&&&&&&#n#n#n#n#n#n#n#n+C#n+C+C+C+C+C+C+++++NNN"! CHELATORS b6W b6 bsbergeeyy3liysky vanayagam m+Zm+[i+\i.%i/i0i0i0i0i0i0i0i0i0i0i1i0i14i15i1Ei1Oi1Ri1bi1ci1di1ei1gi1hi1li1mi1pi1ri1vi1{i1i1i1i1i1i1i1i1i1i1i1i1i1i1i2i2i2i2iAssemblycsgswssssssssQsRsssssssslssssssPss&ssDsHsss=sns~sssss&swssssss s 7s s s s! s!s!s!s!s"s"8s":s"`s"`s2R2222222222222222222222222222222222233333 3 3 3 33333333333 3"3#3$3%3&3333uggests that native DHFR exists in equilibrium with at least one conformer which is recognizable by chaperonin 60. Binding studies with S-35-labeled DHFR support these conclusions and further demonstrate that DHFR competes for a common saturable site with another protein (ribulose-1,5-bisphosphate carboxylase) known to interact with chaperonin 60.Ad^Complex Interactions Between the Chaperonin-60 Molecular Chaperone and Dihydrofolate Reductase Biochemistry3040 9716-97230 8 Oct9|  SubsTrate  T  T X T  T  T  T  T  T T T z T T@ T* T+. T) T T T_ T T T T+ T* T T T. T) T T T TB T"V T$C T$H T$ T$ T$ T% T&T T* T, T, T, T* T&} T-d T-f Th T T- T- T.  T. T. T.? T.N T. T. T. T// T. T/ T0> T, T  T/- T1A T1H T1M T1k T1p T1r T1y T2 T2 T1j T1V T t T3  T3 T3 T4} T4 T4 T5 T5 T5 T5 T5 T6D T6 T6 T6 T6 T6 T7. T76 T7 T7 T8 T8 T T8 T\ s5 s6 s s s s4093 Y3 3 373)G30 0!0!0s020402^0630001)T3SS'B4556.67,78899S1'1P9#9)55555 5 5 5 5;5)5(5 55p55;5)55#5r5{555 75$ 5+l5-B5-51f515152 5556&56-56358555555 5lTetheredr/r ry6'y7i8Xi6'ingya!in ra a8a-aceticl6ZlanineM ; BUTYLAMMONIUMCAINEhloride ODIBENZO%yclined2 e e? e% d d7steiner decameric/p peptide6A saccharidel#ylphosphoglycol ethylammonium fluoroethyl&ahedralE, o6 o$ onY Y Y  Y  Y  Y  Y+ Y Y Y Y  Y4 Yd Yc Y YT Y Y Y" Y% Y.# Y+} Y9]ydroc - c cannabinolnnabinolnNresiduesnn7nn Vn Yn n n xn yn n n pnn)nnnn n5n6n2nXnwnnnnZn`njnnnntn)nnnnnhnnBn~n'nnnnn=nnn nnnnvnnnnnnnGER SOLUTION CONFORMATION TWO-DIMENSIONAL NMR"Clore, G.M. Gronenborn, A.M. 1991piStructures of larger proteins in solution: 3-dimensional and 4-dimensional heteronuclear NMR spectroscopysScienced 252e 5011 1390-1399N 7 JunN 1299ANTENNAPEDIA HOMEODOMAIN AQUEOUS-SOLUTION COUPLING-CONSTANTS INTERPROTON DISTANCE RESTRAINTS MOLECULAR-DYNAMICS N-15-LABELED PROTEINS NUCLEAR MAGNETIC-RESONANCE SOLUTION CONFORMATION STEREOSPECIFIC ASSIGNMENTS TWO-DIMENSIONAL NMR1  & X 732TMBoulat, B. Emsley, L. Muller, N. Corradin, G. Maryanski, J.L. Bodenhausen, G.p 1991zANTIGEN CROSS-RELAXATION RECOGNITION RESONANCE ROTATING-FRAME SEQUENCES SOLID-PHASE SYNTHESIS SPECTRA SPECTROSCOPY T-CELLST lymphocytes expressing variable cell surface antigen receptors recognize "processed" forms of antigen, presented on the surface of other cells by molecules of the major histocompatibility complex (MHC). Naturally processed antigenic peptides can be replaced by synthetic ones. The synthetic peptide AYPPPPPTLA (P5) is an active competitor to the antigenic peptide HLA A24 170-182 (sequence RYLENGKETLQRA) that is recognized by A24 specific T cells in association with the H-2K(d) class I MHC molecule. In P5 the five prolines were designed to play the role of a rigid spacer between the residue Y and the T-L unit, so as to mimic the role of Y171, T178, and L179 in the HLA A24 antigenic peptide, since these residues have proven to be the most important with respect to the binding of the HLA A24 peptide with the H-2K(d) MHC molecule. Nuclear magnetic resonance studies allow us to demonstrate that in aqueous solution P5 adopts at least three long-lived conformations that can be classified with respect to the Y2-P3-P4 amide bonds as trans-trans, cis-trans, and cis-cis. Among these, the trans-trans form is present in 67% of the molecules while the two others share the remaining 33%.{NMR Studies of an Oligoproline-Containing Peptide Analogue That Binds Specifically to the H-2Kd Histocompatibility Molecule Biochemistry3039 9429-94349 1 Oct 733:3Boulat, B. Konrat, R. Burghardt, I. Bodenhausen, G. 1992ASSIGNMENTS SPECTROSCOPY\VMeasurement of Relaxation Rates in Crowded NMR Spectra by Selective Coherence Transfer.(Journal of the American Chemical Society 11413 5412-5414t 17 Jun 734b[Bourdineaud, J.P. Howard, S.P. Pages, J.M. Bernadac, A. Leroy, G. Bruschi, M. Lazdunski, C.i 19902 FERREDOXINS BACTERIAL FERREDOXINS DESULFOVIBRIO-DESULFURICANS NORWAY LOCALIZATION PROTEINS SECRETION SEQUENCE DETERMINATION SITE-DIRECTED MUTAGENESIS STABILITY STRAINd]Cytoplasmic and Periplasmic Expression of a Synthetic Gene for Ferredoxin in Escherichia-Coli7 Biochimie72 6-7407-415Jun-Jul""""""""9999999999&&&&&FFFFFCCCCCCCCCCCCCCC-o-o-o-o-o-ojjjjjjjj,,,,,,444444444MMMMMMMMKKKKK[[[[[[[[[[+hhhhhhhhhhhhhhh+9+9+9+9+9+9+9+9&&&&&&555555555 t|vRRRKRhRRRR]RpR|R} Mann, C.J. Matthews, C.R. 1993Structure and stability of an early folding intermediate of Escherichia coli trp aporepressor measured by far-UV stopped flow circular dichroism and 8-anilino-1-naphthalene sulphonate. Biochemistry32 5282-5290  JAHr 4809,%Mann, C.J. Royer, C.A. Matthews, C.R. 19933-STATE DENATURATION ACID ALPHA-LACTALBUMIN BINDING COOPERATIVITY DIHYDROFOLATE-REDUCTASE FOLDING INTERMEDIATE FOLDING MECHANISM INTERMEDIATE PROTEIN STABILITY PROTEINS PURIFICATION REPRESSOR STABILITY TRYPTOPHAN FLUORESCENCE TRYPTOPHAN MUTATIONSzTryptophan Replacements in the trp Aporepressor from Escherichia-coli - Probing the Equilibrium and Kinetic Folding ModelsProtein Sciences211 1853-18611 Nov3 4807 Mann, C.J. Matthews, C.R. 1993ALPHA-LACTALBUMIN DIHYDROFOLATE-REDUCTASE DNA EQUILIBRIUM FOLDED APOMYOGLOBIN INTERMEDIATE MOLTEN GLOBULE PROTEIN REPRESSOR STATE TRYPTOPHAN-SYNTHETASEfStructure and Stability of an Early Folding Intermediate of Escherichia-coli trp Aporepressor Measured by Far-UV Stopped-Flow Circular Dichroism and 8-Anilino-1-Naphthalene Sulfonate Binding Biochemistry3220 5282-5290 25 May("Mann, C.J. Shao, X. Matthews, C.R. 1995 Characterization of the slow folding reactions of trp aporepressor from E. coli by mutational analysis of prolines and catalysis by a peptidyl-prolyl isomerase. 2 5 H O  Biochemistry34 14573-14580  SJE5 4810(!Mannella, C.A. Guo, X.W. Dias, J.e 1992APOCYTOCHROME-C COMPUTER IMAGE PROCESSING CRYSTALS ELECTRON-MICROSCOPY IMPORT MITOCHONDRIAL CHANNELS MITOCHONDRIAL TARGETING SEQUENCES NEUROSPORA-CRASSA OUTER-MEMBRANE CHANNEL PORIN SIGNAL PEPTIDE VDAC YEAST MUTANTRKBinding of a Synthetic Targeting Peptide to a Mitochondrial Channel Protein 0)Journal of Bioenergetics and Biomembranes 241P 55-61 Febc 4812 Manning, M.C. Woody, R.W. 1987hbTheoretical determination of the CD of proteins containing closely packed antiparallel beta-sheets Biopolymerse2610 1731-1752. Oct0 48112+Manning, M.C. Illangasekare, M. Woody, R.W.  1988`ZCircular dichroism studies of distorted alpha-helices, twisted beta-sheets, and beta turnsBiophysical Chemistry31 1-2 77-86 Aug 4813 Manning, M.C. Woody, R.W. 1989Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor Biochemistry2821 8609-8613R 17 Oct 4814 Manning, M.C. Woody, R.W. 1991ALAMETHICIN ALPHA-HELICES CIRCULAR DICHROIC SPECTRA CONFORMATION DISTORTIONS OLIGOPEPTIDES OPTICAL PROPERTIES POLY L PROLINE PROTEINS VACUUM ULTRAVIOLETnhTheoretical CD Studies of Polypeptide Helices -Examination of Important Electronic and Geometric Factors BiopolymersN315569-586N Apr6 48152+Manningkrieg, U.C. Scherer, P.E. Schatz, G.h 1991HEAT-SHOCK HSP60 HSP70 IDENTIFICATION MEMBER MULTIGENE FAMILY OUTER-MEMBRANE POLYPEPTIDE-CHAIN PRECURSOR PROTEINS REFOLDING TRANSLOCATION YEAST YEAST MITOCHONDRIAVOSequential Action of Mitochondrial Chaperones in Protein Import into the Matrixe EMBO Journal1011 3273-3280 Nov- 48162,Manolios, N. Bonifacino, J.S. Klausner, R.D. 1990ALPHA-CHAIN ANTIGEN RECEPTOR BETA-CHAIN INFLUENZA HEMAGGLUTININ INTRACELLULAR-TRANSPORT MONOCLONAL-ANTIBODIES REQUIRES SUBUNIT SURFACE EXPRESSIONLXRTransmembrane Helical Interactions and the Assembly of the T-Cell Receptor ComplexScience 249M 4966274-277 20 Jul.JAH-n.n.n.n.n.Pn-n-n-nn.nfn.n-n.nnn+Gn-nn}nnNn#xn sn(n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.n.In.:n/nn/nnnn/n&nwnnn& EnzymologyA p  pG pa p p p p p p< p)Z p  p  p  p  p  p v p { p  py p+# p p p p p8 pE pI pH p  p* p p p7 p p pO p p \ p  p" p) p#r p$, p$H p$ p$ p$ p% p& p) p) pC p'T p) p- p% p. p. p. p. p pnn) l)TllllQl mechanism of such remarkable binding, we have characterized complexes between the bacterial chaperone SecB and a series of ligands related to maltose-binding protein. SecB interacts at multiple sites on its polypeptide ligand. The entire binding region covers approximately half of the primary sequence of maltose-binding protein and comprises contiguous sites positioned around the center of the sequence.f the p `@ !( x wT)SJE*SS(S)SS(S+S&S(S*S+S*S(S(SS*S*S*S*SS*eSNS* SSSS(S S'`S RS(S<S S#<S;SFSS*S)S)S+S+SS*pS(S+S*S)S,S,S,S,S,S,S,S,S,S,S,S,S,S,S,S$proteins$R$R)R$R)R$R%R%R% R%R%#R%&R%+R&R%/R%;R%<R%CR%RR%WR%VR%XR%YR%[R%]R%R%R'WR%R%R%R%R%R%R%R%R%R&R&R*-R&BR&LR&ZR&fR&sR)R&R'R'%R)5R))R+gRR iR iR iR iR iR iR iR iR iRW PUrification e e e e e e  e e/ eC e e ) e 4 e 5 e 7 e  e  e  e! e! e!B e!D e!E e!| e!~ e! e" e"$ e"+ e"7 e"Q e"_ e"b e"y e" e" e" e" e# e# e#" e#b e#m e#| e# e$K e$z e$ e$ e$ e%! e%L e%v e% e% e% e% e& e&& e&3 e&A eRatneryss-s0s6lss u u uuuuu\u[u!u$u%uluu/TT"#T+yT/T/T6T6@T6bT6T6T6T6T6T6T6T6T7T7mT7sT8XT8cT6TTUS4'zeburgercu*c&Yc49chb5b7'bbergerg|gei+llston2s ~shelVV5v(vv*rz66sensv%zier!vagnanzzola E E E! EENi& ichandranndra#}shanker8uwyee.e%e*eIeyeyeyelston ~shelV5v(vv*rz%zierv!vagnanzzola E E E! EENi& ichandranndra#}shankeryee%e*eIeye'2181 H2 I2,3 347|912147 .5751125;52 C24b'26'2 2 8b677 4784184W78c8,=87a8 #42401287b8657b88)=99 $9$6 %96r0723+56767$6~9:200 O0 000(0000,0!.0&0-0.002j0980 0 0X0c0P0O0N0)000 &0+07e1111717869772 1 2 62;233 733'4 A44 ?5W5 E659033)=6 F78 4665)A7 58818297277989-x7 17539147 (906o16h29735 5 822827 (90 5 822Q4m)A>HpGz&|--mu-o$&]*!-!b--O=!b+ J(&+$#HOX(6>Z'z*$hWs&!+|#J#5I)pVOi#6['P 9$Hv={-{(%#4(t3(t(tFl6+(1g+!h$;  +T  )*o\_ +bwp)'qa>U+,n #,= Biomedical i) i i8v i) i+o i1D' i1U' i3' s4t' s5k' s5' s5' s7' s2' s7'ina7' e e n n4y'zin+ net+X m+Z m+[ m+\ m+^ m+_ m+` m+a m+b m+c m+d m+e m+f m+g m+h m+i m+j m+k m+l m+o m+p m+q m+r m+w m+x m+y m+{ m+| m+} m+~ m+ m+ m+ m+ m+ m+ m+ m+ m+ m, m+ m+ m+t m+Y m+Y mH Assignments s s s s s s s8 s s s s sW s s s s su s s s J s b s#P s# s# s# s$ s$ s%  s%; s% s+ sF s s s% s!9 s sA sp s s{ s!; s%k s#% s%  s s s s s s  s  s!n s) s$U s+ s+ s+s s6 s8n s8r s8u s8y s8 s8 s8 s8 sOsteeused)f/f@fNf^fffff7ff Sf xf yf f f f f f ff)f)fffMffjfnffff&ff^f ffffffff%ff(ffffffof4f&ff Yf f f!f"4f"Mf"vf"yfh Constrained t t t t t t t tK tq tp to t  t  t"B t" t$ t+ t/ t t5 t6  t . t$ t t t i5 i6 i6 i6U i6b i6r i6 i8U i- ing6 s7 t  t! s$ s_ s u s  s# s9M s s_ s# s s sd s7 s8C s s) U H U  UR U@ U U$ UI U U  U! U! U" U# U# U% U& U+ U,T U  u uuuuuuuuuCCCCCCCCCsCsssssssssssssssssUUUUMUMMMMyyyyyyyyyyyyyyyyiiiiiimmmmmmmmmmjjjjjjj++++%>>>>>>>>>>>>>&&&&&```````````````GGGGssssssssssP$Refsl8{ggaine7eedn(nrr*rr,r,rr/~r2r5]r6r7+r8r'rde e6e7ce&edi7iCing e3 l7 l l  l  l  l5 l7p l8 llessz+y z6Q z6 zGzzienerate&O d> ing onn s s" s% s> s s s s  s2'sburg4<' t7X' tAteing gelin ierMEl8s0s8n`nelli on,rr~/r2r]5r6r+7r'rde e6e&ediCing e3 l7 l l  l  l  l5 llesszy+ zQ6 z6 zGzzienerateO& d> ing onn s s" s% s> s s s s  s2'sburg<4' tAteing gelin ierMEl0s`nelli onon< RElationship. x` x" x  x  x  x  x  x x x x x^ x x xj x xg x] x x x4 xK x x x xs xZ x2 x x x x x!@ x#P x$ x&\ x&h x+ x[ x= x. x1 x2 x3 x3 x%  x5 x5~ x5{ x6 x7 x8p xs x x) s s sL s  s  s s }24878 |99 9955555 5 5555'525!65"55-5253545556 6 0 w00R0Q000000!d0-m0-0N0080 0 0 1 11D6 21D2 2 3<4 5$ 5 66 57 88 9rton1998  Burz1990v Busa19931/ Busch19913 Buscher2001 Busciglio1991 Busconi19945N Busel1980 Bush19911 Bush1991n Bush1991v Bush19944+{ Bush19977 Bushby19922 Bushfield19935NBushueva1980Bushueva1992 Bushweller1991 !< Bushweller1993!; Bushweller1993 *! Bushweller1997 r Buss1990h Bussey1992  Bustamante1992 *' Bustamante1997  DephosphorylationiiiPi#iEi|iiioii!i%i' ii8$iicker`ted ing:onontoleted^d II$I)SI3`I6I mI 8I iQii"Mi%i+gi0ii6i6i6i%ing 8on o-[ o8~ o+ o o$) o oq o# oQ o  o!' oo o0 o6 o7a o,ADH,2AH|,PA@,MAh@d,FAHX,UAHL,A\@,A4@4,@H(,Ap@HP8;`H;`(A8H;`(@8$H8#;`K`H8#;`Ku`H;`H(AxHE`Hx(A ;`HdxKT`?@ ;`HL8?tx88KQH lD|4Hy`xH`xHE=`8HxH`xH(`|u@Ȁ}H yAT`?A}(ASAmeshp)ppp p p p)p :p 9ppppp$pppppppppppp pzpp$pXpppp7pdpp p p)p"p#p)p%p&p&/p&Op+fpp+op,p!;p'Sp+p+tp+sp0p0p5p6 p6p6p@;CIBA Foundation Symposium CIBA Found. Symp. CIBA Found Sympio(#Circulation Circulation Circulationd.84Clinica Chimica Acta Clin. Chim. Acta Clin Chim ActanLIClinical and Experimental Immunology Clin. Exp. Immunol. Clin Exp Immunol,(Clinical Chemistry Clin. Chem. Clin Chemn,)Clinical Genetics Clin. Genet. Clin Genet,&Clinical Research Clin. Res. Clin Res net($Col. Int. C.N.R.S. L'Eau Syst. Biol.s|yCold Spring Harbor Symposia on Quantitative Biology Cold Spring Harb. Symp. Quant. Biol. Cold Spring 0BiPhhmhh"6h,hh0ih1Jh1wh1h1h2h2h2h2h2h2h2h3h3h3h4sh5h6h8Lh8hhh hhh;haaaa*a&Maa a-a#apa6pa6a7a7Pa8.a8La8ta8a8aartiteh%d hw h) h6 hhasicO+O5O7\OOhO_O#e6)e Ӿ  ߤ l Ӱ ӿh P ӴH Ӹ Ӷ ɘ  ʘ ӯ  Ӿx ٨ ` ӹ\  ӳH 4 D ӷ0IOnicz z z zzz2zzzzzzCz- z3z+z8zz'zznzzz z zBzzzzXzozzzz&Kz mz'Qs6s6ss6s7`s8s#sationz  zzable t t t t+ t% t% ttiono' o  o= e> e( e< e ed e e  elecu `p Demmers, J. `J. Haverkamp, et al. (2000). "Electrospray ionization mass spectrometry as a too6gBINDING6mo6vo6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o7o7'o7,o7-o70o74o76o7Eo7Ro7Wo7]o7co7do7fo7mo7no7po7ro7to7vo7xo7zo7}o7o7o7o7o7o7o Dekroon1990 Dekroon1991 Dekroon1991 Dekroon1993 Dekroon1995) Dekroon1995) Dekroon1996) Dekroon1996 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990"T Dekruijff1990 Dekruijff1991 Dekruijff1991 Dekruijff1991#0 Dekruijff1991"U Dekruijff1991 Dekruijff1991 Dekruijff1991g Dekruijff1992 Dekruijff1992 Dekruijff19922002@:The ATPase domain of SecA can form a tetramer in solution."Journal of Molecular Biology 315r4y831-843+ SSG(!den Blaauwen, T. Driessen, A.J.M. 199682Sec-Dependent Preprotein Translocation in BacteriaArchives of Microbiology 165P 1-8JCden Blaauwen, T. Fekkes, P. Dewit, J.G. Kuiper, W. Driessen, A.J.M.  1996PIDomain interactions of the peripheral preprotein translocase subunit SecA  Biochemistry35 11994-12004S6OFOr6Rb6Sb6Tb6Xb6Yb6[b6\b6_b6`b6ab6bb6gb6hb6ib6jb6mb6nb6pb6rb6tb6vb6wb6xb6yb6zb6{b6}b6~b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6b6DBv6A6A6A6A6A6A6A6A6A6A6A7A7A7A7A7A7A7A7A7A7A7A7A7A7A7A7A7A7 A7!A7"A7#A7$A7%A7'A7(A7)A7*A7+A7,A7-A7.A7/A70A71A72A73A74A75A76A77A78A79A7:A7;A7<A7=A7>A7@A7AA7BA7CAC7A99+#+#+#+#ccccccccccccc&&&-S-Sdddd&&&&&&&&&&&&&&&&&&&&&&&;;&;;;;;;;;;;;;;(((lllllllllllllleeeeeeeeeeeeiiiiiiiiiiiiiiiggggggggggggg,,""""""                       z z z z z z zssss)))))))))&$&$&$aaaaaaaaaqqqqqqqqqqqqq(((((((        %~RR%~RRRRRRROOOOOOO!h!h!h!h!h!h( ( ( ( ( ( ##OOOOO-Q-Q-Qggggggggg)))))QQQQQQQBBBBB&&&&&&&)))33666666)))))))####         ,,,,,,,,,,        YYYYY)))))SS5555555555555TTTTTTVVVVVVVVVVooooooojjjjjjjjjj]]99999999999!!!!!!!!!!!+++&{&{&{&{&{&{xxxxx____________+T+T&|&|&|&|&|&|++++++++@@@@@@@@@@))))))))))))kkEkEEEEEEEEE,,,,,,$$$$$$$!b!b#######  l l l l l l l***xxxxxxxxx,,,,-)--3333333+7+7+7+7+7+7EEEE+7EEE+7EEQQQQQQQQQQQQQQQQQQ&&&&&&&&&,,,,,,    !!!!((((($( ( ( ( ( & gggggggggggggkkkkkkkkkkkkkkkk{{{{{{{{{OOOOOOOO eeeeeeeeeeeee,S,S,S,S,S,S,SWWWWWWWWWWWWW!!!!!!!'''''''''&&VVVVVV&&&&&&&&YYYYYY&&&&&&&& &&&& (n(n(n(n(n;;;;;;;xx;xxxxxxxxxxxxxwwww???????????????(q(q1111111----66666666(p(p(p(p(p(pDDDDD%%%((((((((((>>>>UUUUUUUyyyyyyyy**********AAAAAAAAAA@@@@===k Georgopoulos1993] Georgopoulos19939%c Georgopoulos1994  Georgopoulos1996/0 Georgopoulos19962 Georgopoulos1999^2 Georgopoulos2001^ Geourjon1993F Gepner19808 ; Geppert1993 Gerard19909 X Gerard1991 Gerard19929 Gerard1993s Gerard19939 Gerard19933Q Gerber19929 Gerber1993  Gerber19966- Gerber1999` Gerbi1991* Gerbi1998o Gerdes199110 Geremia2000 Gergely1993 Gerhard1992% Gerhard1993 Gerig1991w Gerig1993v Gerig1993* Gerig1997. Gerisch1990"m Gerisch1992 Gerken19939o Gerl19939+ Gerloff1993* Gerloff1993 Gerlt1985E Germain1992  Germain1993 Germain199391 Germain2001) Germeroth1997B Gernert1992# Gernold1991&. Gerogopoulos19949 Geromanos1993 Geromanos1993  Gerothanassis1992  Gerothanassis1992  Gerothanassis1992  Gerothanassis1992W Gerring1989 Gershoni1991 Gershoni1996 Gersonde19765Gersonde1979sGersonde19919I Gerst1993 Gerstein1991Gerstein19929 Gerstein1993 Gerstein1993 Gerstein19943Gerstein1994.eGerstein1999v6Gerstein2000  Gerstle1993+Gerstner1998+]Gerstner19987 Gertler20036i Gervais20003Gervasio2002+ Gervasoni1998-f Gervasoni1998! Geske1992 Geske1994 Gesmar1993 " Gesteland1990  Gether1993  Gething1989  Gething1990 Gething1990 Gething19907b Gething1990 Gething1992  Gething1992 Gething1992 Gething1992 L Gething1992 Gething1993 Gething1993!/ Gething1993 Gething1993 Gething1993, Gething19947 Gething19943 Gething19955 Gething19962 Gething19972 Gething19982 Gething19996 Gething1999 Getman19919  Gettins1986 Gettins1991 Gettins1992  Getzoff1983 Getzoff1992*X Getzoff19974n Getzoff20024Geurtsen2003o Geuze1990 Geuze19932 Gevaert2000 Gevers19922 Geysen19939&+ Geysen199396> Ghadiri1995*G Ghadiri19976N Ghadiri19976 Ghadiri19986+ Ghadiri2001* Ghaemmaghami199824 Ghaemmaghami20000 Ghaemmaghami2001w70 Ghaemmaghami2002 Ghani1993Gharbibenarous1993  Ghelis1982 % Gheorghiu1991 Ghetti19929!C Ghetti19933 Gheuens1992% Ghezzi19939!CGhibaudi199335Ghiggino1982Ghiggino19933  Ghigo1992# Ghigo1992RGhirardi1992/ Ghiringhelli20005Q Ghiron19765R Ghiron1977/ Ghiron19815 Ghiron1984 Ghiron1991  Ghiso1992J Ghiso1992% Ghiso1993 T Ghiso1993 Ghiso1993 Ghisolfi1992  Gho1992! Ghoraishian1991 Ghorpade1993 Ghosaini1988]Ghosaini1988Ghosaini1989sGhosaini1989Ghosaini1990Ghosaini1991-M Ghose19992t Ghose1999/ Ghose2000 Ghosh1992 Ghosh1992  Ghosh1993*X Ghosh1997, Ghosh1998 Ghyselinck1992 zGiaccobi19922 Giaccone1992!CGiaccone19939  Giannakouros1993  Giannattasio1991  Giannelli19933 Gianni20013 Gianni20017 Gianni20037 Gianni20030%Giannini200003Giannini200100Giannoni1999@%rGiardina1977%sGiardina1978Giardina1980Giardina1982 Gibbons1988 Gibbons1991 Gibbons1991 l Gibbons1991  Gibbons1992 Gibbons1992 Gibbons1992 Gibbons1993 R Gibbs1991 Gibbs1991V Gibbs1992  Gibbs1993K Gibbs1993M Gibbs1993L Gibbs1993. Gibbs19966 Gibbs20001 Gibbs20024I Gibbs20025T Gibbs2003.. Giblin19998 Giblin2003 x Gibrat19900  Gibrat1991 #T Gibrat1993 Gibson19899 Gibson19911  Gibson1991  Gibson1991  Gibson19919 Gibson1991 6- Gibson19911 Gibson1992 e Gibson19929 Gibson19922  Gibson1993  Gibson1993 4 Gibson19944Gicquaud1993% Gicquel1991" Gidamis1993Giebeler19929] Giedroc1988[ Giedroc1993 Gielens19924Gierasch19819HGierasch1982l9GGierasch1983orGierasch1984sGierasch1985)Gierasch1985+bGierasch19859FGIERASCH1985ltGierasch1986uGierasch1986 Geromanos1993  Gerothanassis1992  Gerothanassis1992  Gerothanassis1992  Gerothanassis1992W Gerring1989 Gershoni1991 Gershoni1996 Gersonde19765Gersonde1979sGersonde19919I Gerst1993 Gerstein1991Gerstein19929 Gerstein1993 Gerstein1993 Gerstein1994e.Gerstein1999v  Gerstle1993+Gerstner1998]+Gerstner1998+ Gervasoni1998f- Gervasoni1998i- Gervasoni1998! Geske1992 Geske1994 Gesmar1993 " Gesteland1990  Gether1993  Gething1989  Gething1990 Gething1990 Gething1990 Gething1992  Gething1992 Gething1992 Gething1992L Gething1992 Gething1993 Gething1993/! Gething1993 Gething1993 Gething1993, Gething1994 Getman19919  Gettins1986 Gettins1991 Gettins1992  Getzoff1983 Getzoff1992X* Getzoff1997 Geuze1990 Geuze1993 Gevers19922 Geysen19939+& Geysen19939G* Ghadiri1997* Ghaemmaghami1998 Ghani1993Gharbibenarous1993  Ghelis1982 % Gheorghiu1991 Ghetti19929C! Ghetti19933 Gheuens1992% Ghezzi19939C!Ghibaudi19933Ghiggino19933  Ghigo1992# Ghigo1992RGhirardi1992/ Ghiringhelli2000/ Ghiron1981 Ghiron1991  Ghiso1992J Ghiso1992% Ghiso1993T Ghiso1993 Ghiso1993 Ghisolfi1992  Gho1992! Ghoraishian1991 Ghorpade1993 Ghosaini1988]Ghosaini1988Ghosaini1989sGhosaini1989Ghosaini1990Ghosaini1991M- Ghose1999/ Ghose2000 Ghosh1992 Ghosh1992  Ghosh1993X* Ghosh1997, Ghosh1998 Ghyselinck1992 zGiaccobi19922 Giaccone1992C!Giaccone19939  Giannakouros1993  Giannattasio1991  Giannelli1993%0Giannini200000Giannoni1999@r%Giardina1977s%Giardina1978Giardina1980Giardina1982 Gibbons1988 Gibbons1991 Gibbons1991l Gibbons1991  Gibbons1992 Gibbons1992 Gibbons1992 Gibbons1993R Gibbs1991 Gibbs1991V Gibbs1992  Gibbs1993K Gibbs1993M Gibbs1993L Gibbs1993. Gibbs1996.. Giblin1999x Gibrat19900  Gibrat1991 T# Gibrat1993 Gibson19899 Gibson19911  Gibson1991  Gibson1991  Gibson19919 Gibson1991  Gibson1992 e Gibson19929 Gibson19922  Gibson1993  Gibson1993 Gicquaud1993% Gicquel1991" Gidamis1993Giebeler19929] Giedroc1988[ Giedroc1993 Gielens1992rGierasch1984sGierasch1985)Gierasch1985b+Gierasch1985tGierasch1986uGierasch1986asch198618Nbj9*J+$a 5634Nyholm, P.G. Pascher, I. 1993CELL-SURFACE CEREBROSIDE CRYSTAL-STRUCTURE FORCE-FIELD GLYCOSPHINGOLIPIDS H-2 NMR HEADGROUP NUCLEAR MAGNETIC-RESONANCE OLIGOSACCHARIDES PROGRAM MM2nPreferred conformations of the saccharide-ceramide linkage of glucosylceramides with different ceramide structures (normal and hydroxy fatty acids) were investigated by molecular mechanics (MM3) calculations and compared with conformational features obtained for glucosylglycerolipids (diacyl and dialkyl analogues). Relaxed energy map calculations with MM3 were performed for the three bonds (C1'-O1-C1-C2, torsion angles phi, psi, and theta1) of the glucose-ceramide/diglyceride linkage at different values of the dielectric constant. For the phi torsion of the glycosidic C1'-O1 bond the calculations show a strict preference for the +sc range whereas the psi/theta1 energy surface is dependent on the structure of the lipid moiety as well as on the dielectric constant (epsilon). Calculations performed on glucosylceramide with normal and hydroxy fatty acids at epsilon = 4 (bilayer subsurface conditions) show three dominating conformers (psi/theta1 = ap/-sc, -sc/ap, and ap/ap). The ap/-sc conformer, which represents the global energy minimum, is stabilized by polar interactions involving the amide group. The +sc rotamer of theta1 is unfavored in sphingolipids due to a Hassel-Ottar effect involving the sphingosine O3 and O1 oxygen atoms. Comparative calculations on glycosylglycerolipid analogues (ester and ether derivatives) show a distinct preference for the ap rotamer of theta1. An evaluation of the steric hindrance imposed by the surrounding membrane surface shows that in a bilayer arrangement the range of possible conformations for the saccharide-lipid linkage is considerably reduced. The significance of preferred conformations of the saccharide-ceramide linkage for the presentation and recognition of the saccharide chains of glycosphingolipids at the membrane surface is discussed.MOrientation of the Saccharide Chains of Glycolipids at the Membrane Surface - Conformational Analysis of the Glucose Ceramide and the Glucose Glyceride Linkages Using Molecular Mechanics (MM3) Biochemistry325  1225-1234a 9 Feb,&Nymeyer, H. Garca, A.E. Onuchic, J.N. 1998TMFolding funnels and frustration in off-lattice minimalist protein landscapes.VOProceedings of the National Academy of Sciences of the United States of America95 5921-5928 SJEdNymeyer, H Garcia, AE 2003Simulation of the folding equilibrium of a-helical peptides: A comparison of the generalized Born approximation with explicit solvent ) * Proc Natl Acad Sci U S A 10024 13934-13939 Nov 25 KSR 5635"Nystrom, T. Neidhardt, F.C.M 1992zsBACTERIA CHALLENGE ELECTROPHORESIS EXPRESSION GROWTH HEAT-SHOCK INDUCED CROSS PROTECTION K-12 RELA STATIONARY-PHASENrlCloning, Mapping and Nucleotide Sequencing of a Gene Encoding a Universal Stress Protein in Escherichia-ColiMolecular Microbiology6h21 3187-3198 NovO'Brien, MC McKay, DBiThreonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysist 1993J. Biol. Chem.J. Biol. Chem. 24323-24329t 268t32:4http://www.jbc.org/cgi/content/abstract/268/32/24323November 15, 1993XRhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=86633022+O'Brien, M. C. Flaherty, K. M. McKay, D. B.`NHLysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis'pjDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, USA.8663302 J Biol Chem 1996 2712715874-8.omes c in the yeast Saccharomyces cerevisiae&Journal of Biological Chemistry  2655r 2733-2739a 15 Feb 1877 Dunbrack, R.L. Karplus, M. 1993CONFORMATION CONSTRUCTION DIPEPTIDE ENERGY FLEXIBILITY GLOBULAR-PROTEINS MUTATIONS PREDICTION PROTEINS ROTAMERS SEQUENCES SIDE-CHAINS TORSIONAL POTENTIALS\UBackbone-Dependent Rotamer Library for Proteins -Application to Side-Chain Prediction 230o2543-574 20 Mar"Journal of Molecular Biology12011Y1q111111Q11;11 1 .1"1%1%1&1-J1-1-1-1.D1.1,b1.1.1.1.1u121414151616N16[11 10M0y04'0 0)4300&031122331330324304435435363O664393O979409178358903513d9183d93793711 2222&225f'08i'08'0300322323#4433#13$5733$13%6333%13 143323 2ed to long molecular dynamics trajectories of protein simulations. In an application to fatty acid-binding protein in apo-form and with bound palmitate, several protein orifices known from crystal structures have been confirmed to be major portals of solvent-State. s.As.Ms.\s.]s.bsgs.s,s.s.s.ss.s-s.s.s.s.s.s.s.smss/Ns/ks.s']s/YsKs/s/s/s/s/s/s/s/s/s/s.=s0 s0s0s0s0s0s0 s0"s-s/s0s0s0s0ss0s0s0s1As1AsA1sdimented in d. gradients to a position distinct from those contg. mannosyltransferase I (product of the MNN1 gene), a marker enzyme for the Golgi complex. The recovery of intact compartments contg. these enzymes approached 80% after sedimentation. The KEX2 protease and mannosyltransferase I apparently reside within distinct compartments.r 0749-503Xi Yeast51o 25-33ctmYeast KEX2 protease and mannosyltransferase I are localized to distinct compartments of the secretory pathway*******rrrrrrrrrr!!!!!!!!"""""""UUUUkkkkkkkkkkk-p-p-p-p-p-p-p666666ppppp+$$H $!91+ !h+k,=Ye& $L(x'!+y+(\;'_Wv5l,,GIW,/+A#AAAAAAAAAvvvvvvvLLLLLLLLLLLL7777777      ccccccccccccrrrrrrrrrrrrrrrrQQQrQ|||||||yyyyyyyyyyyyyy@@yy@@@@@@@@@@@@-{-{-{-{-{-{-{PPPP+4+4+4+4+4+4(:::::::::::#_#_#_#_#_#_#_== 4T32210`/4.)r.-, 1746D=Dion, A. Linn, C.E. Bradrick, T.D. Georghiou, S. Howell, E.E.o 1993ACTIVE-SITE BINDING CRYSTAL-STRUCTURES FUNCTIONAL-ROLE MECHANISM METHOTREXATE PROTEIN-STRUCTURE SMALL UNILAMELLAR VESICLES TRIMETHOPRIM ULTRAVIOLET CIRCULAR-DICHROISMHow Do Mutations at Phenylalanine-153 and Isoleucine-155 Partially Suppress the Effects of the Aspartate-27 -> Serine Mutation in Escherichia-Coli Dihydrofolate Reductase Biochemistry3213 3479-3487 6 Apr 1747@:Diprimo, C. Hoa, G.H.B. Deprez, E. Douzou, P. Sligar, S.G. 1993CARBON-MONOXIDE CRYSTAL-STRUCTURE FLASH-PHOTOLYSIS GEMINATE RECOMBINATION HEME-PROTEINS LIGAND-BINDING PSEUDOMONAS-PUTIDA CYTOCHROME-P-450 SITE-DIRECTED MUTAGENESIS SPERM WHALE MYOGLOBIN SPIN EQUILIBRIUM`ZConformational Dynamics of Cytochrome-P-450(cam) as Monitored by Photoacoustic Calorimetry Biochemistry3214 3671-3676` 13 Apr 1748<5Dirago, J.P. Macadre, C. Lazowska, J. Slonimski, P.P. 1993CYTOCHROME BC1 COMPLEX ASSEMBLY GENE GENETICS INTRONS MITOCHONDRION MUTANTS MUTATION MUTATIONS PROTEINS REDUCTASE RESISTANCE RHODOBACTER-SPHAEROIDES SACCHAROMYCES-CEREVISIAE SEQUENCE YEAST{The C-Terminal Domain of Yeast Cytochrome-b Is Essential for a Correct Assembly of the Mitochondrial Cytochrome bc1 Complex FEBS Letters 328 1-20153-158 9 AugXQDistefano, M.D. Kuang, H. Davies, R.R. Qi, D. Miller, L.A. Ory, J. Banaszak, L.J. 1999RKSemisynthetic Approaches for the Design of Proteins with Catalytic Activity Fields, G. Barany, G. &16th American Peptide Symposium "Minneapolis, Minnesota, USA in press1 1:4FABP, covalent modification of FABP, designed enzyme.'Distefano, M.D. Zhong, A. Cochran, A.G. 2002r-Quantifying b-sheet stablity by phage display    "Journal of Molecular Biology 322179-188 JAH 1749VPDistel, B. Gould, S.J. Voornbrouwer, T. Vanderberg, M. Tabak, H.F. Subramani, S. 1992{EXPRESSION FIREFLY LUCIFERASE GENE MICROBODIES PEROXISOME PROTEIN SACCHAROMYCES-CEREVISIAE SEQUENCE SYSTEM TARGETING SIGNALTThe Carboxyl-Terminal Tripeptide Serine-Lysine-Leucine of Firefly Luciferase Is Necessary But Not Sufficient for Peroxisomal Import in Yeast New Biologistc4S2157-165 Feb2 1750(!Divita, G. Restle, T. Goody, R.S.  1993b\DIMERIZATION DOMAIN HIV INTRINSIC PROTEIN FLUORESCENCE REVERSE-TRANSCRIPTASE SUBUNIT BINDING|Characterization of the Dimerization Process of HIV-1 Reverse Transcriptase Heterodimer Using Intrinsic Protein Fluorescence FEBS Letters 324a2153-158o 14 Jun 1752 Dixon, M.M. Matthews, B.W. 1989TNIs gamma-chymotrypsin a tetrapeptide acyl-enzyme adduct of alpha-chymotrypsin? Biochemistry2817 7033-7038e 22 Aug SJE 1751.(Dixon, M.M. Brennan, R.G. Matthews, B.W. 1991Structure of gamma-chymotrypsin in the range pH 2.0 to pH 10.5 suggests that gamma-chymotrypsin is a covalent acyl-enzyme adduct at low pH82International Journal of Biological Macromolecules132. 89-96 Apr 1753HADixon, M.M. Nicholson, H. Shewchuk, L. Baase, W.A. Matthews, B.W.s 1992BOUND WATER CAVITIES CONFORMATIONS DOMAIN MOTION DYNAMICS HYDROPHOBIC STABILIZATION LYSOZYME PARAMETERS PHAGE-T4 LYSOZYME PROTEIN STRUCTURES REFINEMENT RESOLUTION STABILITY T4 LYSOZYME THERMOSTABILITYNHStructure of a Hinge-Bending Bacteriophage-T4 Lysozyme Mutant, Ile3->Pro 2273 917-933 5 Oct"Journal of Molecular Biology 1754Dixon, M.T. Hillis, D.M. 1993f_EVOLUTIONARY LATIMERIA PHYLOGENY RECONSTRUCTION RIBOSOMAL-RNA SECONDARY STRUCTURE SEQUENCE DATAleRibosomal RNA Secondary Structure - Compensatory Mutations and Implications for Phylogenetic AnalysisN&Molecular Biology and EvolutionE101c256-267  Jan      2622Gimble, F.S. Sauer, R.T. 1989TNLambda repressor mutants that are better substrates for RecA-mediated cleavage 2061o 29-39` 5 Mar"Journal of Molecular Biology 2623Gimond, C. Aumailley, M. 1992rkCellular Interactions with the Extracellular Matrix Are Coupled to Diverse Transmembrane Signaling Pathways  Experimental Cell Research 203 2365-373 Dec  2624"Ginsburg, A. Zolkiewski, M.a 1991ADENYLYLATION BINDING-SITE BIOLOGICAL THERMODYNAMIC DATA CALIBRATION DOMAINS HEAT-CAPACITY DATA PROTEINS SEQUENCE STABILITY TEMPERATURE82Partial unfolding of dodecameric glutamine synthetase (GS) from Escherichia coli has been studied by differential scanning calorimetry (DSC). A single endotherm (t(m) = 51.6 +/- 0.1-degrees-C and DELTA-H(cal) = 211 +/- 4 kcal/mol of enzyme) was observed in DSC experiments with Mn.GS in the presence of 1.0 mM free Mn2+ and 100 mM KCl at pH 7. The dodecameric structure of Mn.GS was retained throughout heating cycles, and thermal transitions were reversible as shown by rescans [with 6-18 mg of GS (M(r) 622000) from 15 to 68-degrees-C at 20-60-degrees-C/h] and by > 93% recovery of activity. A cooperative ratio DELTA-H(cal)/DELTA-H(vH) of 1.6 +/- 0.1 and deconvolution analysis show two cooperative units (two-state transitions): t1 = 50.4 and t2 = 51.7-degrees-C; the ratio of the relative sizes of thermally labile domains is approximately 1:2 as judged by DELTA-H-2/DELTA-H-1 congruent-to 2. However, the thermally induced overall enthalpy change (0.34 cal/g) for GS dodecamer is only 5-10% of that for thermal unfolding of small globular proteins at 50-degrees-C. The t1 and t2 values from deconvolutions of DSC data agree with t0.5 values previously calculated from spectral measurements of temperature-induced exposures of approximately 0.7 of 2 Trp and approximately 2 of 17 Tyr per subunit, respectively [Shrake et al. (1989) Biochemistry 28, 6281-6294], over a 14-degrees-C temperature range using both stabilizing and destablizing conditions for Mn.GS. No uncoupling of Trp and Tyr exposures or of cooperative units in DSC experiments with Mn.GS occurred in the presence of either 150 mM Gln (t(m) = 58.6-degrees-C) or 10 mM free [Mn2+] (t(m) = 43.9-degrees-C). Thus, cooperative interactions apparently link partial unfolding reactions of all subunits within the GS dodecamer so that only two two-state transitions are observed.Differential Scanning Calorimetry Study of Reversible, Partial Unfolding Transitions in Dodecameric Glutamine Synthetase from Escherichia-Coli Biochemistry3039 9421-9429 1 Oct.Giorini, S. Galili, G. 1991<6Characterization of HSP-70 Cognate Proteins from Wheat& Theoretical and Applied Genetics825615-620 2625BIP GRP-78 CATALYSTS CHAIN BINDING-PROTEIN CHAPERONE CHLOROPLASTS ELECTROPHORETIC TRANSFER ESCHERICHIA-COLI DNAK HSP70 MAJOR HEAT-SHOCK MEMBER MITOCHONDRIAL PROTEIN NITROCELLULOSE POLYACRYLAMIDE GELS TRITICUM-AESTIVUM WHEAT 26266/Gippert, G.P. Yip, P.F. Wright, P.E. Case, D.A.r 1990CHEMICAL-SHIFTS GEOMETRY MOLECULAR-DYNAMICS NOE NUCLEAR MAGNETIC-RESONANCE OVERHAUSER EFFECT SPECTRA PROTON DISTANCE CONSTRAINTS RELAXATION MATRIX APPROACH SPECTROSCOPY SPIN DIFFUSIONLFComputational Methods for Determining Protein Structures from NMR DataBiochemical Pharmacology401p 15-22i 1 Jul 2627VPGiraldosuarez, R. Fernandeztresguerres, E. Diazorejas, R. Malki, A. Kohiyama, M. 1993rkBACTERIOPHAGE-LAMBDA ESCHERICHIA-COLI GRPE INITIATION INVITRO NUCLEOPROTEIN STRUCTURES ORIGIN ORIR R1 ROLESA|vThe Heat-Shock Dnak Protein Is Required for Plasmid-R1 Replication and It Is Dispensable for Plasmid ColE1 ReplicationNucleic Acids Research2123 5495-5499p 25 Nov~~~~~~~~~~~~~******$$$$$$ttttt'r'r'r@@@@@$++$$DDDDDDDDDDIIIIII++++++)$)$)$%%%%%%%}}!7!7!7!7!7!7!7!7!7*g*g*g $FAnd$Me$We$Xe$]e$e$e$e$e$e$e$e%e%"e%.e%0e%<e%Ce%We%Ze%`e%ue%e%e%e%e%e%e%e%e%e%e%e%e(e%e%e)e%e&e&e&e& e&e&$e&*e&3e&Ze&re&se&|e&e&e'e'#e' e)Ie+eeeeeee,HJ,Ka,Ma,Na,Oa,Pa,Qaa a,Va+a,Ya+a,\a,]a,^a,ca,ea&a+a&a&a)a,va,wa,a,a,a,a,}a,aaa,a,aba,a,a,a,a+a,a,a9a,a,aa,a,aa#aa,a,a,a,a,a,a,a,a,a,a,a,aFunctions=aKa~aaaaaaaaaJaSawaaaa#aeaaaaaaa%a8aGaIaaaaraaaDaRaQa+5aaaaa aIaaaaaaaWa a a a!(a!/a!a!a!a*Ta*Ta,Ofc,N,N,N,N,N*N,N,N,N-N-N-N+N- N- NN#vNNN NN*N)SN)RN(N-N-N-N-N-N-"NNFN-$N-%N-&NNN*N'NNNN?N CN N'N'N'N'N'N'N'N'N'N'N'N'N'N'N'N'N'NEE c c c c c c c c c cH cHHHHHHHH2222222&~&~+)+)+)) ) ) ) ) ) ) ) rrrrrrrCCCCCC,,,,,gggg&&&&&&&&mmmmm,,,,," ++++&!Journal& u&u(u&%u&'u&*u&,u&.u&/u*-u&5u&6u&?u&;u&Mu&Iu&Gu&Tu&Vu&Uu&Zu&au&du&u&u&hu&u&u&vu&uu&su&~u&u&u&u&u&u&u&u&u&u&u&u'u'u'$u'%u'&u+Hu+Ku+Lu+Mu+Nu+Ou+Su+Uu+Vu+Vu+Vu+Vu+Vu+Vu 4199& Kuwajima, K. Ogawa, Y. Sugai, S. 1979jcApplication of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumini Biochemistry185878-882 6 Mar 4197& Kuwajima, K. Nitta, K. Sugai, S. 1980zsIntramolecular perturbation of tryptophans induced by the protonation of ionizable groups in goat alpha-lactalbuminr$Biochimica et Biophysica Actam 623N2389-401 26 Jun 4200& Kuwaji/ BIochemistry5E i5G i5F i5I i5H i5Q i5R i5l i5k i5j i5i i5h i5g i5f i5m i5q i5p i5o i5 i5 i/ i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i5 i6  i6 i6 i6" i6K i6M i6S i6` i6v i6w i6 i6 i6 i6 i6 i6 i6 i6 i6 i7 i7 i7- i72 i79 i7I i7h i7i i7j i7 i7 i7 i7 i7 i7 i7 i7 i8 i8 i1 i8. i81 i85 i8B i8N i8v i8z i8 i8 i8 i8 i8 i8 i8 i8 i6 i9  i/ i9< i i i- i- i- i8/ i iT i8 i  i& i6 i i i i  i i- i iT i8 i  i& i6 i i i i  i i&IInm&Hc&Oc(c&Wc&ac&c&c&hc&c&c&rc&wc&vc&uc&zc&c&c&c&c)c&c&c&c&c'#c'&c+Kc+Nc+Qc+Sc+Uc+Vc)+c),c)-c) c)#c+[ccuc+_c+`crc+bc'Kc+eccc+gcc&c* ccQc(c(c(c(c(c(c(c(c(cz rJAcqe3 'ues3intSottdotegern&h*hRhningnickeff Af f rfffffffff f fBfff fffjfif.f_fkfff f#f%Of%ff&ffff/f3xf4<s6s7s s08schffe)rik"ggadishnnnadham e,thd1e0e7ueendorfh hr2Wm5m6Jmminas2 226APafniolactose{ktionov 0mbeejmadnaduP riepy TEdyE2270@l ssanet tt6tt3t t t rUrrrrrrrrsral$t te}stUtVtictessVtic-b-b-b-b-b!z!z!z!znnnnnnnnnnmmmmmmmmJJJJJJJJ+ + + "0"0"0"0"0-         ;;;;&&&&&&         $$$$$$$$$$$$#$########## F+48'[R8 197nhArcher, D.B. Jeenes, D.J. MacKenzie, D.A. Brightwell, G. Lambert, N. Lowe, G. Radford, S.E. Dobson, C.M. 1990 0733-222XErkHen egg white lysozyme expressed in, and secreted from, Aspergillus niger is correctly processed and foldedu88 741-745p Biotechnologyp2,Archer, S.J. Ikura, M. Torchia, D.A. Bax, A. 1991mAn alternative 3D NMR technique for correlating backbone 15N with side chain Hb resonances in larger proteinsT 9  ; N P $Journal of Magnetic Resonanceh95636-6411 201<5Archer, S.J. Vinson, V.K. Pollard, T.D. Torchia, D.A. 1993~ACTIN ASSIGNMENTS C-13 COHERENCE GELSOLIN LARGER PROTEINS N-15 NMR N-15-LABELED PROTEINS PHOSPHOLIPASE-C PHYSARUM-POLYCEPHALUMSecondary Structure and Topology of Acanthamoeba Profilin-I as Determined by Heteronuclear Nuclear Magnetic Resonance Spectroscopy Biochemistry3226 6680-6687r 6 Juli 200Archer, S.J. Bax, A. Roberts, A.B. Sporn, M.B. Ogawa, Y. Piez, K.A. Weatherbee, J.A. Tsang, M.L.S. Lucas, R. Zheng, B.L. Wenker, J. Torchia, D.A.J 19932D 3-DIMENSIONAL STRUCTURES INTERLEUKIN 1 BETA MULTIPLE-QUANTUM COHERENCE NMR-SPECTROSCOPY PEPTIDE-BOND PROTEIN-STRUCTURE SPECTRA STAPHYLOCOCCAL NUCLEASE TGF-BETA|vTransforming Growth Factor-beta-1 - Secondary Structure as Determined by Heteronuclear Magnetic Resonance Spectroscopy Biochemistry324 1164-1171 2 Feb  199Archer, S.J. Bax, A. Roberts, A.B. Sporn, M.B. Ogawa, Y. Piez, K.A. Weatherbee, J.A. Tsang, M.L.S. Lucas, R. Zheng, B.L. Wenker, J. Torchia, D.A.C 19933-DIMENSIONAL HETERONUCLEAR NMR C-13 COHERENCE-TRANSFER FACTOR-BETA H-1-NMR SPECTRA INTERLEUKIN 1 BETA LARGER PROTEINS MAGNETIC-RESONANCE SPECTROSCOPY N-15 SEQUENCETransforming Growth Factor-beta-1 - NMR Signal Assignments of the Recombinant Protein Expressed and Isotopically Enriched Using Chinese Hamster Ovary Cellse Biochemistry3241 1152-11631 2 FebJCArcus, V.L. Vuilleumier, S. Freund, S.M.V. Bycroft, M. Fersht, A.R. 1995A comparison of the pH, urea, and temperature-denatured states of barnase byu heteronuclear NMR: implications for the initiation of protein folding."Journal of Molecular Biology 254305-321 SJEd 203PJArdail, D. Privat, J.P. Egretcharlier, M. Levrat, C. Lerme, F. Louisot, P. 1990CHOLESTEROL DIPHENYLHEXATRIENE FLUIDITY FLUORESCENCE DEPOLARIZATION FLUOROPHORES HEXOKINASE MEMBRANES OUTER SPONTANEOUS EXCHANGE VESICLESB8Jorgensen, S.M. Whitlock, S.V. Thomas, P.J. Ritman, E.L. 19920*Dynamic image-adaptive x-ray beam limiters264S328-334TJul-Augp0)Biomedical Instrumentation and Technologyy 3659B;Jorgensen, A.M.M. Kristensen, S.M. Led, J.J. Balschmidt, P.u 19922D H-1-NMR 2D NMR COUPLING-CONSTANTS CROSS-RELAXATION DES PENTAPEPTIDE INSULIN DIMER INSULIN MONOMERIC INSULIN PROTEIN SECONDARY STRUCTURE SOLUTION STRUCTURE SPECTRA STRUCTURE CALCULATION TIME-DOMAIN DATA TWO-DIMENSIONAL NMR3-Dimensional Solution Structure of an Insulin Dimer -A Study of the B9(Asp) Mutant of Human Insulin Using Nuclear Magnetic Resonance, Distance Geometry and Restrained Molecular Dynamics 227 4 1146-1163 20 Oct"Journal of Molecular Biology 3662*#Joseph, D. Petsko, G.A. Karplus, M. 1990VPENERGY ENZYME MOLECULAR-DYNAMICS SIMULATIONS PROTEINS TRIOSE PHOSPHATE ISOMERASEb\Anatomy of a Conformational Change - Hinged Lid Motion of the Triosephosphate Isomerase LoopScience 249c 4975 1425-1428 21 SepJoseph, M. Nagaraj, R. 1992haUnfolding of Lysozyme by Breaking Its Disulphide Bridges Results in Exposure of Hydrophobic Sites Biochemistry266973-978 May 3664VOBINDING EXPORT IMPORT MEMBRANES MITOCHONDRIA POLYPEPTIDES PROTEIN TRANSLOCATION 3663 Joseph, D.R. Lawrence, W.0 1993rlAMINO-ACID SEQUENCE CELLS ENDOCYTOSIS EPIDIDYMIS ESTRADIOL EXPRESSION IDENTIFICATION PROTOMERS RECEPTOR SITEpiMutagenesis of Essential Functional Residues of Rat Androgen-Binding Protein/Sex Hormone-Binding GlobulinMolecular Endocrinology974p488-496 Apr("Joseph, S. Weiser, B. Noller, H.F. 1997B7Joshi, H.C. Palacios, M.J. McNamara, L. Cleveland, D.W. 1992ALPHA-TUBULIN ANTIBODY ASPERGILLUS-NIDULANS FILAMENTS HAMSTER OVARY CELLS IDENTIFICATION INITIATION LYSED MAMMALIAN-CELLS MITOTIC CENTERS SPINDLEf_gamma-Tubulin Is a Centrosomal Protein Required for Cell Cycle-Dependent Microtubule Nucleation  Nature 356 6364 80-83 5 Mar 36672+Joshibarve, S. Debenedetti, A. Rhoads, R.E.i 1992f`BINDING CAP COMPLEX FACTOR-III INACTIVATION INHIBITION INTERNAL INITIATION LEADER SEQUENCE VIRUSPreferential Translation of Heat Shock messenger RNAs in HeLa Cells Deficient in Protein Synthesis Initiation Factors eIF-4E and eIF-4gammae&Journal of Biological Chemistry  26729 21038-21043  15 Oct 36686/Joslyn, G. Richardson, D.S. White, R. Alber, T.. 1993ADENOMATOUS POLYPOSIS-COLI CHROMOSOME-5Q21 COLON CANCER FAMILIAL ADENOMATOUS POLYPOSIS FAP GENE HEPTAD REPEAT REGION IDENTIFICATION LEUCINE-ZIPPER LOCUS MUTATIONS SUBDOMAINF?Dimer Formation by an N-Terminal Coiled Coil in the APC Proteind9023 11109-111135 1 Dec1VOProceedings of the National Academy of Sciences of the United States of America 3669`YJoy, J.E. Johnson, G.S. Lazar, T. Ralph, M.R. Hochstrasser, A.C. Menaker, M. Merril, C.R. 19922-DIMENSIONAL ELECTROPHORESIS BIOLOGICAL RHYTHMS CIRCADIAN PACEMAKER CIRCADIAN RHYTHMS DROSOPHILA CLOCK ELECTROPHORESIS EXPRESSION MESSENGER-RNA PERIOD GENE-PRODUCT PROTEIN RAT-BRAIN SUPRACHIASMATIC NUCLEUS SYSTEM TAU-MUTANT HAMSTERJDProtein Differences in tau-Mutant Hamsters -Candidate Clock ProteinsMolecular Brain Research15 1-2 8-14 Sep1 8F*FZ110HADD 1789JDDoma60Driessen, A. J. Fekkes, P. van der Wolk, J. P. 1998The Sec system.2Curr Opin Microbiolt1r2 216-222960Driessen, A. J. Manting, E. H. van der Does, C. 2001NGThe structural basis of protein targeting and translocation in bacteriai Nature Structural Biology 8e6i 492-8 SSGtDriessen, A.J. 20010*SecB, a molecular chaperone with two facesTrends Microbiol9c5193-196 May SSGr 1850<6Driscoll, P.C. Gronenborn, A.M. Beress, L. Clore, G.M. 1989Determination of the three-dimensional solution structure of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: a study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing Biochemistry285T 2188-2198T 1849<6Driscoll, P.C. Clore, G.M. Beress, L. Gronenborn, A.M. 1989A proton nuclear magnetic resonance study of the antihypertensive and antiviral protein BDS-I from the sea anemone Anemonia sulcata: sequential and stereospecific resonance assignment and secondary structurei Biochemistry285 2178-2187 18512+Driscoll, P.C. Gronenborn, A.M. Clore, G.M.r 1989The influence of stereospecific assignments on the determination of three-dimensional structures of proteins by nuclear magnetic resonance spectroscopy. Application to the sea anemone protein BDS-Iy FEBS Letters 243d2223-233LFDriscoll, P.C. Clore, G.M. Marion, D. Wingfield, P.T. Gronenborn, A.M. 1990Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1 beta Using Three-Dimensional Heteronuclear NMR Spectroscopy Biochemistry29 3542-3556o SJEB;Driscoll, P.C. Gronenborn, A.M. Wingfield, P.T. Clore, G.M. 1990Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy Biochemistry2919 4668-4682 15 May 1848 SJE 1847rlDriscoll, P.C. Altman, J.D. Boniface, J.J. Sakaguchi, K. Reay, P.A. Omichinski, J.G. Appella, E. Davis, M.M. 1993BINDING C 13 LABELING CHEMICAL-SHIFTS CLASS-II MHC CONFORMATION ISOTOPE-EDITED NMR SPECTROSCOPY MHC MULTIPLE-QUANTUM COHERENCE NMR PH-DEPENDENCE PROTEIN-PEPTIDE COMPLEX PROTEINS PROTON RECOGNITION SPECTROSCOPY 2-Dimensional Nuclear Magnetic Resonance Analysis of a Labeled Peptide Bound to a Class-II Major Histocompatibility Complex Molecule 2322r342-350s 20 Jul"Journal of Molecular BiologyZSDrohat, A.C. Amburgey, J.C. Abildgaard, F. Starich, M.R. Baldisseri, D. Weber, D.J.  1996VPSolution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy Biochemistry3536 11577-11588dpro-OmpA. Translocation required ATP, SecY, and SecA and was stimulated by a protonmotive force. These results provide an important assay for the isolation and identification of membrane components involved in protein translocation. 0027-8424TleSolubilization and functional reconstitution of the protein-translocation enzymes of Escherichia coli878 3107-3111&Los Angeles, CA 90024-1737, USAVOProceedings of the National Academy of Sciences of the United States of AmericaoP Pauling1951 Pauling1976% Paulsen19923G Paulsen20024]Paulucci2002 Pauptit1991 Pauptit19925U Pauthe2003 Paver1989 Pavesi1993 SPavirani199112 Pavletich19972 Pavletich19986 Pavletich20003 Pavletich20020 Pavlik2000 Pavone1992  Pavone1992  Pavone19920 Pavone20000 Pawson19922 Pawson19929 Pawson19921 Pawson19929 Pawson19939 Pawson19939 Pawson199492 Pawson20022 Payan1991 Payan1992 Payan1992 Payne1991 Payne1993 Payne1993!s Payne1993$ Payne1993+ Payne19982 Payne20009` Payne2004B Paz1992 Pazmany19928^ Pazos2002 Peak19933 Pearce1996 2 Pearl19972 Pearl19972 Pearl19994 Pearl19992 Pearl20004g Pearl2002+ Pearlstone1998 , Pearse19818 Pearse1984  Pearse1988  Pearse1990 Pearson1968: Pearson1992 Pearson1993 Pearson1993( Pearson1994)G Pearson1997 Pease1988 Pease1990 Pease1991 Pease1993 Peattie1991 Peattie1992 Pebaypeyroula1992 Pebaypeyroula1993 Peccoud1990 Pechan1991  Pecht1979) Pecht1998 Peckmiller1993 Pecorari1993.Pecorari1996o Pedelaborde1992Pedersen1989 Pedersen1990 dPedersen1990Pedersen1990Pedersen1991!Pedersen1991i "Pedersen1991Pedersen1991Pedersen1992!Pedersen1992!Pedersen1992!Pedersen1992i!Pedersen1992!Pedersen19925Pedersen1992nPedersen1993Pedersen1993#Pedersen19933%Pedersen1993Pedersen1993!Pedersen1993QPedersen1994!Pedersen1995*Pedersen1998-)Pederson1996 Pedone19929 Pedone19922 Pedone19921& Pedone19933& Pedone19971p Pedrazzini1995 3 Pedroso2002 Peek1992v Peelen1992 ) Peelen1996  Peeler19909 Peeler1993 F Peemoeller1991  Peerce1991  Peersen1992 Peersen1992#M Peeters1991X Peggion1990W Peggion19901 Peggion1999 Pegna1992 Pegna1992 Pegna19932Pegoraro200003 Pei20024G Pei20028! 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Peltier1992 Pelton19919  Pelton1991  Pelton1992 _ Pelton19939 Pelton1993 > Pelton1996/ Pelton20000 Peltz1991/ Pelupessy20000 Peluso20001" Peluso20017 Peluso2001 Pemberton1988 Pemberton1988  Pemberton1989 Pemberton1989&4 Pemberton1990*6 Penczek19977_ Penczek20017 Penczek2001 S Pendelbury1992  Pendleton1993  Peng19929 Peng1992v Peng19939 Peng1993v Peng1994 Peng1994v Peng1995v] Peng19951%d Peng1995v'( Peng19961** Peng19988* Peng1998v6 Peng1998/Z Peng19999/Y Peng2000/ Peng2000 / Peng2000t5 Peng20006 Peng2000t6 Peng200002> Peng200113| Peng20018 Peng2001135 Peng200223 Peng200224 Peng20020+ Penin1993 Penington1992 Penington1992 Penke1992( Penkett1997/ Penkett2000 Penn199229 Penn20044. Penning1998*] Pennisi1997  Penno1993- Penzes1999#c Pepermans1990 Pepperkok1991 Pepperkok1993 - Pepperkok1993 Pepys1988 Pepys1993& Pepys1997% Perahia1990Perakyla1992 Peralta1990 Peralta19936 Peralta1993 Peralta1994/Perkyl20004Percival1992  Percivalsmith1990ivalsmith1990n1997 Pease1988 Pease1990 Pease1991 Pease1993 Peattie1991 Peattie1992 Pebaypeyroula1992 Pebaypeyroula1993 Peccoud1990 Pechan1991  Pecht1979) Pecht1998 Peckmiller1993 Pecorari1993.Pecorari1996o Pedelaborde1992Pedersen1989 Pedersen1990 dPedersen1990Pedersen1990Pedersen1991!Pedersen1991i "Pedersen1991Pedersen1991Pedersen1992!Pedersen1992!Pedersen1992!Pedersen1992!Pedersen1992i!Pedersen1992!Pedersen19925Pedersen1992nPedersen1993Pedersen1993#Pedersen19933%Pedersen1993Pedersen1993!Pedersen1993QPedersen1994!Pedersen1995*Pedersen1998-)Pederson1996 Pedone19929 Pedone19922 Pedone19921& Pedone19933& Pedone19971p Pedrazzini1995  Peek1992v Peelen1992 ) Peelen1996  Peeler19909 Peeler1993 F Peemoeller1991  Peerce1991  Peersen1992 Peersen1992#M Peeters1991X Peggion1990W Peggion1990 Pegna1992 Pegna1992 Pegna1993/ Peisajovich2000Peishoff1991~Peishoff19922Peishoff1992 Peishoff199220 Peitsch19960 Peitsch1997Peitzsch1993 Pekar1992 Pekar1993 Pelcher1990 Pelech1992 Peled1993- Pelham1986 Pelham1990  Pelham1991 Pelham19929 Pelham1992 Pelham1992 !# Pelham1992  Pelham19939 Pelicci1992 Pelicci1992  Pelicci1992 Pelicci1992  Pellecchia1996- Pellecchia1999/ Pellecchia2000+! Pellechia1997+  Pellechia1998  Pellequer19930 Pelletier2001! Peltier1992 Pelton19919  Pelton1991  Pelton1992 _ Pelton19939 Pelton1993 > Pelton1996/ Pelton20000 Peltz1991/ Pelupessy20000 Peluso2000 Pemberton1988 Pemberton1988  Pemberton1989 Pemberton1989&4 Pemberton1990*6 Penczek1997 S Pendelbury1992  Pendleton1993  Peng19929 Peng1992v Peng19939 Peng1993v Peng1994 Peng1994v Peng1995v] Peng19951%d Peng1995v'( Peng19961** Peng19988* Peng1998v/Z Peng19999/Y Peng2000/ Peng2000 / Peng2000t/ Peng20000+ Penin1993 Penington1992 Penington1992 Penke1992( Penkett1997/ Penkett2000 Penn19922. Penning1998*] Pennisi1997  Penno1993- Penzes1999#c Pepermans1990 Pepperkok1991 Pepperkok1993 - Pepperkok1993 Pepys1988 Pepys1993& Pepys1997% Perahia1990Perakyla1992 Peralta1990 Peralta1993 Peralta1994/Perkyl20004Percival1992  Percivalsmith199090   Pt+h 241 Asher, S.A. 1993AROMATIC AMINO ACIDS CROSS-SECTIONS EXCITATION PROFILES EXCITED-STATE N-METHYLACETAMIDE PEPTIDE-BOND SATURATION SPECTROSCOPY SPECTRA TRYPTOPHAN TYROSINE\VUV Resonance Raman Spectroscopy for Analytical, Physical, and Biophysical Chemistry .2Analytical Chemistry654 A201-A210 15 Feb 240 Asher, S.A. 19930*DYNAMICS EXCITATION LASER SCATTERING STATE\VUV Resonance Raman Spectroscopy for Analytical, Physical, and Biophysical Chemistry .1Analytical Chemistry652A59-A66 15 Jan<5Ashton, D.S. Beddell, C.R. Green, B.N. Oliver, R.W.A. 1994haRapid validation of molecular structures of biological samples by electrospray-mass spectrometry.D 342 1-6| FEBS Letters>7Askin, D. Bloomberg, G.B. Chambers, E.J. Tanner, M.J.A.X 1998pjNMR Solution Structure of a Cytoplasmic Surface Loop of the Human Red Blood Cell Anion Transporter, Band 3 Biochemistry37 11670-11678 242JCAssamunt, N. Mortishiresmith, R.J. Aurora, R. Herr, W. Wright, P.E. 1993ANTENNAPEDIA HOMEODOMAIN CAENORHABDITIS-ELEGANS CRYSTAL-STRUCTURE HEAVY-CHAIN PROMOTER IMMUNOGLOBULIN GENES NMR-SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE PROTEIN CONFORMATIONS REGULATORY PROTEINS TRANSCRIPTION FACTORThe Solution Structure of the Oct-1 POU-Specific Domain Reveals a Striking Similarity to the Bacteriophage-lambda Repressor DNA-Binding Domain Cell731l193-205 9 Apr- 243Ataka, M. Asai, M. 1990CRYSTALLIZATION PROTEINSf_Analysis of the Nucleation and Crystal Growth Kinetics of Lysozyme by a Theory of Self-AssemblyUBiophysical JournalR583807-811- Sep  244 Atencio, D.P. Yaffe, M.P. 1992ESCHERICHIA-COLI GENE HEAT-SHOCK PROTEIN HSP70 NUCLEOTIDE-SEQUENCE PRECURSOR PROTEIN PROCESSING PROTEASE SACCHAROMYCES-CEREVISIAE STRESS PROTEINS TRANSLOCATIONPLFMAS5, a Yeast Homolog of dnaJ Involved in Mitochondrial Protein Import$Molecular and Cellular Biology121y283-291 Jan 246@9Atkins, W.M. Cader, B.M. Hemmingsen, J. Villafranca, J.J. 1993CONFORMATION DECAY ENZYME ENZYME-ACTIVITY EPSILON-AMP ESCHERICHIA-COLI LOOP MODULATION FLUOROMETRY MOLECULAR-DYNAMICS MUTANTS PHASE PROTEINS RESOLUTION SEQUENCE TRYPTOPHANTime-Resolved Fluorescence and Computational Studies of Adenylylated Glutamine Synthetase - Analysis of Intersubunit Interactions2Protein Sciencet2n5800-813n May0 245*#Atkins, A.R. Martin, R.C. Smith, R. 1995$DISULFIDE NMR STRUCTURE TOXINc~1H NMR Studies of Sarafotoxin SRTb, a Nonselective Endothelin Receptor Agonist, and IRL 1620, an ETB Receptor-Specific Agonist Biochemistry34 2026-2033n 2480*Atkinson, M.A. Maclaren, N.K. Scharp, D.W. 199060No Role for 65 kD Heat-Shock Protein in Diabetes Lancet 336O 8725 1250-1251 17 Nov 247HBAtkinson, M.A. Holmes, L.A. Scharp, D.W. Lacy, P.E. Maclaren, N.K. 19914.ANTIGEN AUTOANTIBODIES BACTERIAL GROEL PROTEINnhNo Evidence for Serological Autoimmunity to Islet Cell Heat Shock Proteins in Insulin Dependent Diabetes(!Journal of Clinical Investigationl872t721-724S Feb 249 Atkinson, S.J. Stewart, M. 1992CHARGED COMPLEMENTATION ESCHERICHIA-COLI EXPRESSION FRAGMENTS LIGHT-MEROMYOSIN MOLECULAR INTERACTIONS MUSCLE MUTAGENESIS MYOSIN ASSEMBLY PARACRYSTALS PROTEINS REGIONNb[Molecular Interactions in Myosin Assembly - Role of the 28-Residue Charge Repeat in the Rodv 226v1 7-13 5 Jul2"Journal of Molecular Biology  0Ah.s  231:3Arrowsmith, C. Pachter, R. Altman, R. Jardetzky, O. 1991ASSIGNMENT CRYSTAL-STRUCTURE DNA-BINDING HEURISTIC REFINEMENT METHOD LARGER PROTEINS MAGNETIC-RESONANCE DATA NMR DATA OPERATOR SEQUENCE SPECTROSCOPYWe have determined the solution structures and examined the dynamics of the Escherichia coli trp repressor (a 25-kDa dimer), with and without the co-repressor L-tryptophan, from NMR data. This is the largest protein structure thus far determined by NMR. To obtain a set of data sufficient for a structure determination it was essential to resort to isotopic spectral editing. Line broadening observed in this molecular mass range precludes for the most part the measurement of coupling constants and stereospecific assignments, with the inevitable result that the attainable resolution of the final structure will be somewhat lower than the resolution reported for smaller proteins and peptides. Nevertheless the general topology of the protein can be deduced from the subsets of NOEs defining the secondary and tertiary structure, providing a basis for further refinement using the full set of NOEs and energy minimization. We report here (a) an intermediate resolution structure that can be deduced from NMR data, covalent, angular and van-der-Waals constraints only, without resort to detailed energy calculations, and (b) the limits of uncertainty within which this structure is valid. An examination of these structures combined with backbone amide exchange data shows that even at this resolution three important conclusions can be drawn: (a) the protein structure changes upon binding tryptophan; (b) the putative DNA binding region is much more flexible than the core of the molecule, with backbone amide proton exchange rates 1000 times faster than in the core; (c) the binding of tryptophan stabilizes the repressor molecule, which is reflected in both the appearance of additional NOEs, and in the slowing of backbone proton exchange rates by factors of 3-10.rlThe Solution Structures of Escherichia-coli-trp Repressor and trp Aporepressor at an Intermediate Resolution& European Journal of Biochemistry 202y1 53-66 15 Nov 232D>Artymiuk, P.J. Grindley, H.M. Kumar, K. Rice, D.W. Willett, P. 1993ACTIN AIDS ATPASE FOLD COMPLEX CRYSTAL-STRUCTURE ESCHERICHIA-COLI FRAGMENT GRAPH THEORY HIV PROTEIN STRUCTURES RECOGNITION REVERSE-TRANSCRIPTASE RIBONUCLEASE-H SECONDARY STRUCTURE STRUCTURAL SIMILARITYs3-Dimensional Structural Resemblance Between the Ribonuclease-H and Connection Domains of HIV Reverse Transcriptase and the ATPase Fold Revealed Using Graph Theoretical Techniquesh FEBS Letters 324f1 15-21r 7 June<5Artymiuk, P.J. Poirrette, A.R. Rice, D.W. Willett, P.{ 1997.(A polymerase I palm in adenylyl cyclase? Nature 388  33-34 233B;Arvidsson, K. Land, T. Langel, U. Bartfai, T. Ehrenberg, A.e 1993DISTANCE CONSTRAINTS GLOBULAR PROTEIN MOLECULAR-DYNAMICS NUCLEAR MAGNETIC-RESONANCE PANCREATIC-POLYPEPTIDE PROTON NMR SECONDARY STRUCTURE SOLUTION CONFORMATION SPECTRA SPINAL CORDEpiSolution Structure by 2D H-1-NMR of a Chimeric Peptide Recognized by Galanin and Neuropeptide-Y Receptorsn Biochemistry3230 7787-7798 3 AugU 235Arvinte, T. Drake, A.F. 19932-DIMENSIONAL NMR ANALOGS AUTORADIOGRAPHY BIOLOGICAL-ACTIVITY H 1 NMR INTEGRAL-EQUATIONS MODEL PEPTIDE RECEPTORS SKELETAL SOLUTION CONFORMATION-voComparative Study of Human and Salmon Calcitonin Secondary Structure in Solutions with Low Dielectric Constants &Journal of Biological Chemistry6 268 9 6408-6414 25 Mar 234& Arvinte, T. Cudd, A. Drake, A.F. 1993AMIDE-I AMYLOID FIBRILS DISEASE FLUORESCEIN GELATION MEDULLARY CARCINOMA NUCLEATION PROTEINS SECONDARY STRUCTURE SICKLE-CELL HEMOGLOBINTJDThe Structure and Mechanism of Formation of Human Calcitonin Fibrils&Journal of Biological Chemistrye 2689R 6415-6422l 25 Mar 236(!Asada, T. Sonobe, S. Shibaoka, H.s 1991INVITROVPMicrotubule Translocation in the Cytokinetic Apparatus of Cultured Tobacco Cells Nature 350  6315238-241 21 Mar.(Asada, S. Koide, T. Yasui, H. Nagata, K. 1999JDEffect of Hsp47 on prolyl 4-hydroxylation of collagen model peptides"Cell Structure and Functiond24187-196  JAHd 237&Asai, K. Hayamizu, S. Handa, K.c 1993JDPrediction of Protein Secondary Structure by the Hidden Markov Model.(Computer Applications in the Biosciences92141-146d Apr 238tmAsano, T. Takata, K. Katagiri, H. Tsukuda, K. Lin, J.L. Ishihara, H. Inukai, K. Hirano, H. Yazaki, Y. Oka, Y.t 1992TNBRAIN CELLS GLUT4 INSULIN PLASMA-MEMBRANE PROTEINS SIGNAL TISSUE TRANSLOCATIONXRDomains Responsible for the Differential Targeting of Glucose Transporter Isoforms&Journal of Biological Chemistry 26727 19636-19641f 25 Sep 239$Ashendel, C.L. Boutwell, R.K.p 1981{Direct measurement of specific binding of highly lipophilic phorbol diester to mouse epidermal membranes using cold acetoneL:3Biochemical and Biophysical Research Communications992543-549 31 Mar@ Liket 0l!Cl"l"l#l$/l$sl$l$l%ll*l+l*l,*l,-l+ll-3l-gl-l-l-l-l-Hl.l.l/l/l/l/l/lul0l/l-l1xl1l2(l2sl2l2l2l2l3:l3Hl3_l3l3l4l43l4el4rl4l4l4l)l4l5l5l5l6l6_l6l7lilllllll           ! " # $ % & ' ( ) * + , - . / 0 1 2 3 4 5 6 7 8 9 %nuclear%%%%%%& &0&1&DY&Cu&A&J&H&UE&Z}&h&&&u)&&)5)()1+`r+d+e'O+l)D)!u+p)2)'T+y#+|+}+~++++++++ \-'%bw" Y@ %Htl!D-C ,,  `! ! $ 5@$( (!$1 eကA!f 9!0,DA1m-T-Ą   @ 0H O%$!& "%& $ŀ@% % !`p    $m j!̀@ ))`!  @`13!C$%AC%!/$ED$ % g% jA#Biology#t$3$ q$o$"a$#m$+ $4r$6i$;t$K$`$a$n$o$$$$*($$$$$+6$$$$$$$$$)%+%/&%8*%L%M%W%^%d%f%r%s%a%a%a%a%a%a%a%a%a%a%a%ae into the lipid film is evidenced by a rapid rise in film pressure. Spectroscopic results obtained on films transferred to quartz plates and Ge crystals show that the peptide is a mixture of alpha-helix and beta-conformation where the long axis of the alpha-helix penetrates the monolayer plane and the beta-structure is coplanar with the film. By contrast, when peptide is injected under lipid at high initial pressure, no pressure rise is observed, and the spectroscopic results show the presence of only be( INtermediate o o} o oZ o~ o oQ oe on om o~ o o o o o o o' o( o o ) o 9 o  o  o = o E o [ o r o& o  o Q o  oQ o o o oK o- o o= o o. o o o o# o( o( o( o( o o o o o o o o o o oLOBIN BOVINE SERUM-ALBUMIN CIRCULAR-DICHROISM DOMAIN-SIZED FRAGMENTS GUANIDINE-HYDROCHLORIDE HEME MYOGLOBIN PROTEINS SECONDARY STRUCTURE SODIUM DODECYL-SULFATE SURFACTANT UREANSecondary Structural Changes of Metmyoglobin and Apomyoglobin in Anionic and Cationic Surfactant Solutions - Effect of the Hydrophobic Chain Length of the Surfactant on the Structural Changes "Journal of Protein Chemistry116.583-588 Dec Ҭ >$ 5299D>Morita, E.H. Shirakawa, M. Hay%K%a%a%a%a%a%a)a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a&a&a&a&a& a&a&a&'a&2a&4a&;a&Oa*a&ca&a&{a&a&a&a'"a'#a'%a'%a'%a'%a'%a'%a+Ca+Ea+Ea Nelson1993  Nelson1993  Nelson1993 *\ Nelson1997 NelsonNOV 1992 Nemens19929$2Nemerson1993 Nemethy1990# Nemethy1993) Nemthy1977 Nemmers1992 Nemoto1992  Nemoto1993  Nepomuceno1993 O Neri1991k Neri1991v Neri1991v$ Neri19911 P Neri19922!9 Neri1992p Neri19921 Neri1992v Neri1992v Neri1992v Nesmeyanova1991 Nesmeyanova vut2=D/q.psqdop*;nFm 3392@:Huth, J.R. Mountjoy, K. Perini, F. Bedows, E. Ruddon, R.W. 1992jdBINDING CHORIOCARCINOMA CELLS FORM INTERMEDIATE LYSOZYME NMR PATHWAY REGION RIBONUCLEASE-A SECRETIONDomain-Dependent Protein Folding Is Indicated by the Intracellular Kinetics of Disulfide Bond Formation of Human Chorionic Gonadotropin-beta Subunit&Journal of Biological Chemistryy 26730 21396-21403 25 Oct 3393B;Huth, J.R. Perini, F. Lockridge, O. Bedows, E. Ruddon, R.W.l 1993ASPARAGINE-LINKED OLIGOSACCHARIDES BIOLOGICAL-ACTIVITY BOND FORMATION CHORIOCARCINOMA CELLS ENDOPLASMIC-RETICULUM MICROSOMAL-MEMBRANES PANCREATIC TRYPSIN-INHIBITOR SECRETION SERUM-ALBUMIN SUBUNITProtein Folding and Assembly Invitro Parallel Intracellular Folding and Assembly - Catalysis of Folding and Assembly of the Human Chorionic Gonadotropin alpha-beta Dimer by Protein Disulfide Isomerase&Journal of Biological Chemistrye 26822 16472-16482  5 AugZSHuth, J.R. Bewley, C.A. Jackson, B.M. Hinnebusch, A.G. Clore, G.M. Gronenborn, A.M.* 1997xrDesign of an expression system for detecting folded protein domains and mapping macromolecular interactions by NMRProtein Science6 2359-2364  SSG 3395*#Huttner, W.B. Gerdes, H.H. Rosa, P. 1991ADRENAL-MEDULLA CELLS IMMUNOCYTOCHEMICAL LOCALIZATION MESSENGER-RNA MONOCLONAL-ANTIBODY HISL-19 PANCREASTATIN PEPTIDES PITUITARY SECRETORY PROTEINS COMMON TERMINAL FRAGMENT4.The Granin (Chromogranin/Secretogranin) Family$Trends in Biochemical Sciences161y 27-30 Jan.(Huyghues-Despointes, B.M.P. Nelson, J.W. 1992JDStabilities of Disulfide Bond Intermediates in the Folding of Apamin Biochemistry315d 1476-1483 11 Feb 3397AMINO-ACIDS DEPENDENCE EXCHANGE HELIX DIPOLE MODEL NUCLEAR MAGNETIC-RESONANCE PANCREATIC TRYPSIN-INHIBITOR PATHWAY PEPTIDE PROTEINS RIBONUCLEASE-A>7Huyghues-Despointes, B.M.P. Scholtz, J.M. Baldwin, R.L. 1993piEffect of a single aspartate on helix stability at different positions in a neutral alanine-based peptideVProtein Science210 1604-1611 Oct 3399ALPHA-HELIX COIL TRANSITION DIPOLE MODEL HELIX DIPOLE HELIX PROPENSITY HYDROGEN BONDING PROTEINS STABILIZATION VARYING CHAIN LENGTHS 3396<5Huyghues-Despointes, B.M. Scholtz, J.M. Baldwin, R.L. 1993nhHelical peptides with three pairs of Asp-Arg and Glu-Arg residues in different orientations and spacingsProtein ScienceY2M1 80-85T Jan:4Huyghues-Despointes, B.M.P. Scholtz, J.M. Pace, C.N. 1999XQProtein conformational stabilities can be determined from hydrogen exchange rates Nature Structural Biology610910-912JAH SJEVOHuyghues-Despointes, B.M.P. Langhorst, U. Steyaert, J. Pace, C.N. Scholtz, J.M. 1999|vHydrogen-exchange stabilities of RNase T1 and variants with buried and solvent exposed Ala->Gly mutations in the helix Biochemistry38 16481-16490 SJEdLFHuyghues-Despointes, B. M. Pace, C. N. Englander, S. W. Scholtz, J. M. 2001NHMeasuring the conformational stability of a protein by hydrogen exchangeMethods Mol Biol 168 69-9211357629 JAHZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11357629Hvidt, A. Nielsen, S.O. 1966$Hydrogen exchange in proteins5$Advances in Protein Chemistry521287-386 JAH  3401*#Hwang, D.S. Crooke, E. Kornberg, A. 1990BACTERIOPHAGE-LAMBDA ENZYMATIC REPLICATION ENZYMES ESCHERICHIA-COLI CHROMOSOME GENE HEAT-SHOCK PROTEINS INITIATION PROTEIN ORIGINpiAggregated dnaA Protein Is Dissociated and Activated for DNA Replication by Phospholipase or dnaK Protein&Journal of Biological Chemistry 26531 19244-19248  5 Nov 3402Hwang, D.S. Kaguni, J.M. 1991AUTO-REGULATION AUTOPHOSPHORYLATING ACTIVITY BACTERIOPHAGE-LAMBDA CHROMOSOME-REPLICATION DELTA-DNAK52 MUTANTS HEAT-SHOCK PROTEINS INITIATION PROTEIN NORMAL GROWTH TEMPERATURES NUCLEOPROTEIN STRUCTURES PLASMID MAINTENANCE`YdnaK Protein Stimulates a Mutant Form of Dnaa Protein in Escherichia-Coli DNA Replication.&Journal of Biological Chemistry9 26612 7537-75412 25 Apr7uupone7|p7~p7p7p7p7p7p7p7p7p7p7p7p8p8$p8*p85p8Yp8dp8lp8wp8p8p8p8p8p4'pen2bergr+r, R3RR%R$R61R6hRR8Le2 egulation6NightsHOCKt5'tatemhreamqt tt%tt tTtXt#t$tt6yt7Ct7t4taketake7p7p7p7p7p7p7p7p7p7p7p7p7p8p8$p8*p85p8Yp8dp8lp8wp8p4'pen2bergr+r, R3RR%R$R61R6hRR8Le2 egulation6NightsHOCKt5'tatemhreamqt tt%tt tTtXt#t$tt6yt7Ct7t4takeT$axis mmm m+am6;m6Mm6Nm6[m6`m6{m8dm8ym8m&manno(ojona9aa4a3a3a)aa_a3a a$a?a)alSfSSjSLSS2SSSLS S' SSrS4SXS-SS S! S!"S"S$e#.emalS#S)SPPPPLASMI3IICY- Y qYae-ede1m4-m*Bmerichr%r                                   2Uid2P2P2P2P2P2P2P2P2P2P2P2P1jP1VP2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P1>P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P OF MERCHANTABILITY AND FITNESS FOR A PARTICULAR PURPOSE OR THAT THE USE OF THIS SOFTWARE OR DATA WILL NOT INFRINGE ANY THIRD PARTY PATENTS, COPYRIGHTS, TRADEMARKS OF OTHER RIGHTS. NLM Downloading Policy The material in the Medline and Medline-derived databases contains material from copyrighted publications and users are therefore advised that downloading for re-distribution is subject to copyright restrictions. NLM does, however, permit downloading of the citation and MeSH terms for a small number539-540 Jul 11122,Chaudhuri, B. Helliwell, S.B. Priestle, J.P. 1991BINDING BIP SECRETION CATALYSTS DIMERIZATION FOLDING MALFOLDING INVIVO GENE INSULIN-LIKE GROWTH FACTOR-1 INTERMOLECULAR DISULFIDE BOND LUMINAL ER PROTEINS SACCHAROMYCES-CEREVISIAE SEQUENCEA Lys27-to-Glu27 Mutation in the Human Insulin-Like Growth Factor-1 Prevents Disulfide Linked Dimerization and Allows Secretion of BiP When Expressed in Yeast FEBS Letters 2943M213-216e 9 Decp!% Birkenmeier1988!$ Birkenmeier1988  Birkenmeier1989y Birkenmeier1989j Birkenmeier1989  Birkenmeier1991k Birkenmeier1991 Birkenmeier1991 Birkenmeier1991  Birkenmeier1991*Birktoft1998  Birlirakis19929  Birlirakis19929z Birmes1990 KBirnbaum199336 Birney19999{ Biro1990v- Birolo1999| Birse1996+f Birse1997 Bishop1985  Bishop1986e Bishop1987e Bishop19877m Bishop19900'2 Bishop19911# Bishop19922} Bismuto1992 Bismuto1993~ Bismuto1993 Bismuto1994 Biswas1992 5k Biswas200335k Biswas200330 Bitan20010 Bitter2001 7q Bitter2001Bittersuermann1993 Bixler1992  Bizot1993 Bizzi1989& Bizzini1993$ Bjorck19933 Bjork1992 Bjork1993% Bjork19963g Bjork2002% Bjorkdahl1996+wBjorkman1987Bjorkman19929 Bjorkroth1992 Bjorksten19711 Bjorndahl2002 Bjornholm19933 Bjrk20024 Blaas2003 Blaber19929 Blaber1993  Blaber19935 Blaber2003 Black19927c Black1992 Black1993)+ Black1997.g Black1998. Black19997f Black1999 Blackbourn1993 6 Blackburn2000 Blackledge19929*+Blacklow1997  Blackshear1989  Blackshear1992  Blackshear1993 j Blackwell1992/= Blackwell19979 Blackwood1999 Blades19929 Blades199296 Blaha2003 Blake1965 Blake1990&4 Blake1990% Blake1991 Blake1992 Blake1992! Blake1992, Blake1992 Blake1993 Blake1993! Blake1993- Blake1993 Blake1996& Blake19973 Blake2002 Blakley1993V Blalock19904 Blalock1993 Blanchard1992) Blanchard1995 Blanck19871 Blanco1992  Blanco1992 ! Blanco19922^ Blanco19922 Blanco1993 Blanco19939: Blanco1993 r Blanco1993 _ Blanco19939 Blanco19946 Blanco1994 Blanco1995 ; Blanco1995 ) Blanco19955) Blanco1996a( Blanco1997a0\ Blanco199795 Blanco19977+ Blanco19984 Blanco1998-T Blanco19997d Blanco2001 Blancuzzi1993. 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Blobel1995 ) Blobel1995 ) Blobel19955) Blobel1995) Blobel1995) Blobel19966*6 Blobel19979* Blobel199897_ Blobel200117 Blobel200118Z Blobel20030 Blochet1992s Blochmann1993 Block1991! Block1993* Block1998/ Bloemendal1989#- Bloemendal1990  Bloemendal19921  Bloemendal1992  Bloemendal1993 Bloemendal19931Blokzijl1993c Blom19929 Blom1993vBlomberg1992Blomberg1993Blomhoff1993gBlommers19969 Blomquist1993 Blomquist19932 Blond19982 Blond19988 Blond19991 Blond20001J Blond20011 Blond2001Blond-Elguindi1988Blond-Elguindi1990Blond-Elguindi1990Blond-Elguindi1993Blond-Elguindi19933Blond-Elguindi1995 Blondel1990 Blondel1993 Blondelle1992 Blondelle1992 Blondelle1992 Blondelle1995,Z Blondelle1997? Bloom1990> Bloom1990 Bloom1990 Bloom1990 Bloom1992 Bloom1992 Bloom1993 Bloom1993 Bloom1993* Bloom1998+ Bloomberg199819929*+Blacklow1997  Blackshear1989  Blackshear1992  Blackshear1993 j Blackwell1992 Blades19929 Blades19929 Blake1965 Blake1990&4 Blake1990% Blake1991 Blake1992 Blake1992! 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Bloom1990> Bloom1990 Bloom1990 Bloom1990 Bloom1992 Bloom1992 Bloom1993 Bloom1993 Bloom1993* Bloom1998+ Bloomberg199898erg19980271&02'0D0&3f1&2 2"3-3&3'-3'5, 405'5"5&6&677'7 8&9&9*2D999!999P9O995u9)T9(95 5 =5 4&00)90)700W0!k0(0))0)20*0+00,V0(0,0,0)S0-0&}0-e0.{0'S0.00\0):0)?020/!020*06060606070708080'00&1*1, 2-2'2'2)3042''repeatskiyi{i i i gi iisi)i.iii#i#i&fi+Oi+i+i+>ii1@i2i2i2i2i3i4i6i7iTii'5i)i iEEE!E"E#E#@E&5E&6E+oE6E?EQE+e,eNe6-e6ae6e6e7e7 e8eedi#i6ii&ii3ii$ti&iAi7l8l6elyiing f s$t s5 sL s, sTstqt t Rt3t(t&t%t, BIochemistry,  i+< i* i* i( i* i* iV i i'` i  i R i( i( i) i; iF i i* i, i+F i+ i+ i,# i+ i+ i,& i,' i+- i+, i,( i,) i,* i,+ i,, i+ i,- i) i,. i,/ i,0 i,2 i+ i,7 i i,: i,; i,< i* i* i i i i i i i i i i i i 1tangles 2u 3u 4u 6u du u 5u u u u uuuuuu|uuucubuduujuuu&uuuuuuCuuuuNu u=uuuuuuu(u 6u!6u!>u!Cu!Yu#u$(u$u%5u%u6auuuu27rot4Yu9uayi:gT R Octapeptide s6 s s6 o8| o+RoberP+?P+>P,P,P0P0P0P1P1P PINEusOy.y5xynol5ylY5Y1YY#pphenylY9YTOCINd yz d3'a7ann{nzn-4k|kan"YnniyPyNdefeyn3n'Qnse8t" intsova.UMRvxoevskayamn}n~nnnnnnell e>oghueF e/irantiedemaS 1 1 1 1)1 1 1 O1 x1 1 1 1 161E1*141121w1&1x1111&11111111;1<1>1x11 1 11 1R1$1111^1_1o11711 1"E1"y1#/1#z1#1#1)&1+Z1+Z14G1L111(1^11t11Y1111n111 1:1]1o1111n1o1v1z1y1{11111111111111 1w11 $1 }1 1 1!|1!1"L1"1"1"1#1$V1$s1$1%1%1&f1f&1EINS MOLECULAR-DYNAMICS NMR NUCLEAR MAGNETIC-RESONANCE REPRESSOR SECONDARY STRUCTURE SIMULATED ANNEALING SOLUTION STRUCTURE TRP REPRESSORS\VRefined Solution Structures of the Escherichia-Coli trp Holorepressor and Aporepressor 229 3735-746y 5 Feb-"Journal of Molecular Biology 8808Zhelev, D.V. Needham, D. 1993CELL-MEMBRANES CONTACT ELECTRICAL BREAKDOWN ELECTROPERMEABILIZATION ELECTROPORATION FIELD FUSION LINE TENSION LIPID BILAYER-MEMBRANES LIPOSOME-D/2)2x2t2u22"2#'2#$2#%2/?2.H2.=2020 2/20202/20220 20&2*20/20320620720820:20Q220T20[20M2)2/20^20f20j2220u20x20z20}20202020202020202020202020202020202DEOXYRIBONUCLEICROOOO!eO#QO%xOv OPROTEINS} spergualin}t thymidinepRIDECANUCLEOTIDEe7'parment6'tament7' o7' o7' o7' o3' o4]' e4v' e5' e6+' e2'ement2' m73' m7' m85' m8' mmente) e) e) e)G C)$ C) C) C& C)H C) C) C) C) C)% C)& C)6 C)4 C)+ C)1 C)* C+^ C+_ C+a C+d C+e C'O C'J C+h C+i C+j C+l C& C) C+q C'P C)2 C+r C'M C+w C) C'T C  !  ( ("*} ﾺﻫ $@"(!!!!!!*******           %%%%%%%%%%%%%(l(l(((((((((((ZZZZZZZZZZZZZZZZZ+++++++++++>>>>>>>>>uuuuuuuuuuuuuuuu---------//////$$/$$$$$OOOOOOOOOOO(m(m(m(m(m(m(m. Components sK sT s  s' s s s sf sJ s\ s> sA sy s s s s< s s s s s/ s sP s s s"1 s"v s" s+K st s.m s/9 s6 s7{ s7 s sP sS s& s s  s  s8 s~ s+ s s! s6 sM s s s  s s s$ s s s s s s s s s  s! s structure d) d? d d d$ d d d d d d d' d d dM da d d d d d d)G d  d  d} d d% de d d d d d d d d d dl d d d# d^ d_ do dC dd d& d d d Y d _ d  d  d!o d!n d) d! d! d"C d"y d"y d+eM+fM'OM'JM)DMM)*M ampp S SCp p+f68+f729)-s+fA),A)-A+fA!A|DBs}s)-s))TTbYYzS|AAAbbburnal of Biological Chemistry 26815 10760-107655 25 May 8843$Zielenkiewicz, P. Saenger, W.J 1992ZSAREAS ENERGY FORCE-FIELDS GLOBULAR-PROTEINS HYDROPHOBICITY LYSOZYME SURFACE VOLUMESRmaynnnnn&nnnn6nRnnn n Sn Vn mn n gn 9e xe e ee6ee4eDereweDD&bXbZb`bbbb^b]bbbbbbbbbbbbbb bbbMbbbbbbpppp ;p#pp mp14*-46yamycin H e  e DT D  p!O p pportQDD)eQrseedSHANUSidoDlFlfll$lkllney\ssono mp1mamycin H e  e D DportQDQerHHANUSidoDlFlfll$lkllTRANSP" ESCHERICHIA# p# p# p#, p#O p#S p#^ p#_ p#q p#t p#z p#| p# p# p# p# p# p$ p$ p$& p$' p$/ p$: p$? p$K p$O p$_ p$b p$s p$ p$ p$ p$ p$ p$ p$ p$ p% p%  p% p% p% p% p% p%! p%' p%/ p%e p%v p% p% p% p% p% p% p% p% p% p% p% p% p% p a i  i) iN i)1 i+\ i+o iing p s s s" s$r s$q s p s s"2 s% s+i ss[ G+ G G G/ G/ Gudied MUC1 related peptides with a type I beta-turn identified in the region PDTR. This portion of the peptide has previously been identified as the binding site for the monoclonal antibodies HMFG-1 and HMFG-2. The peptide where the D has been replaced by its homologue E, which is selectively recoSOmewhat#qy5y7yhyamjm%m%m`mer io o o*o&+meyer villeogyi n-r rjain/sennard d d3/tore _dek l l l!l-gl wl1[rmann2 h.hignn:IIIII I I I I!I$~i*i,i,i)[i1Ui1Wi2i3i4i6i!icatedn%Z n n%ionWnenberg6hammer ichsen  o* o o  o3 oobe3 oobe9Siteesss-gss(ssJ JyJ&Oz+<V V-KV VczeJJE $SS%S:SSS!SSS'S-SSSSS S S%nSSJE/keletaliny"$ovgaard Lightly~owl+edlMalluoI#erhItho oothNANyder&ociGietyl Llld%dd Cd*ddiumj$jad 0lid%csDs+ ubilizationleTionfvs sAs&s sss-SBiology,,,-N-;-T-U-V-W-X-Y-Z-k-m-n-o,-r-s-v-y- +  , }$l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|N xH؀tH̀pHlHhHdH`H\HXHxTHlPH`LHTHHHDH<@H0<H$8H4H 8`N 8`N |ܐ!;#;D;e;;;CX8z:<8H;<;HHe`(@ 8`H|(@A䐤(,@ 8`NG CONTACT SITES TRANSCARBAMYLASE TRANSPORTntnRole for the Mitochondrial Inner Membrane in the Maturation of the Precursor to Ornithine Carbamyl Transferase:3Biochemical and Biophysical Research Communications3 170C3 1273-1280 16 Aug 1394"Cotterill, S.M. Fersht, A.R. 1983|Direct observation of complexes of ssb and recA proteins with a fluorescent single-stranded deoxyribonucleic acid derivative Biochemistry2225 5878-5881d 6 Decqqqqqqqqq!]!]!]!]((((((%x%x%x,6,6,6,6,6,6,6,6++++++55555"""""""****kkkkkkk***((((((*******pppppppppp)|)|)|)|)| qB4%opnlkij0gh 8} 12033872ngDetailed unfolding and folding of gaseous ubiquitin ions characterized by electron capture dissociationThe unfolding enthalpy of the native state of ubiquitin in solution is 5 to 8 times that of its gaseous ions, as determined by electron capture dissociation (ECD) mass spectrometry. Although two-state folding occurs in solution, the three-state gaseous process proposed for this by Clemmer and co-workers based on ion mobility data is supported in general by ECD mass spectra, including relative product yields, distinct Delta H(unfolding) values between states, site-specific melting temperatures, and folding kinetics indicating a cooperative process. ECD also confirms that the 13+ ions represent separate conformers, possibly with side-chain solvated alpha-helical structures. However, the ECD data on the noncovalent bonding in the 5+ to 13+ ions, determined overall in 69 of the 75 interresidue sites, shows that thermal unfolding proceeds via a diversity of intermediates whose conformational characteristics also depend on charge site locations. As occurs with increased acidity in solution, adding 6 protons to the 5+ ions completely destroys their tertiary noncovalent bonding. However, solvation of the newly protonated sites to the backbone instead increases the stability of the secondary structure (possibly an alpha-helix) of these gaseous ions, while in solution these new sites aid denaturation by solvation in the aqueous medium. Extensive ion equilibration can lead to even more compact and diverse conformers. The three-state unfolding of gaseous ubiquitin appears to involve ensembles of individual chain conformations in a "folding funnel" of parallel reaction paths. This also provides a further caution for characterizing solution conformers from their gas-phase behavior.'|uDepartment of Chemistry and Chemical Biology, Baker Laboratory, Cornell University, Ithaca, New York 14853-1301, USA.nD=Breuker, K. Oh, H. Horn, D. M. Cerda, B. A. McLafferty, F. W.eng Journal ArticleAmino Acid Sequence Gases Ions Kinetics Molecular Sequence Data Protein Conformation Protein Folding Spectrum Analysis, Mass/methods Support, U.S. Gov't, P.H.S. Thermodynamics Ubiquitin/*chemistry J Am Chem Soc  2002 Jun 5 124 226407-20. 814@9Breukink, E. Demel, R.A. De Korte-Kool, G. De Kruijff, B. 1992.'INTERACTION LIPID MEMBRANE PROTEIN SECArSecA-lipid interactions are believed to be important for the translocation of precursor proteins across the inner membrane of Escherichia coli. SecA insertion into the phospholipid bilayer could play a role in this process. The authors investigated this possibility by studying the interactions between SecA and different phospholipids using the monolayer technique. It was established the SecA is surface-active and can insert into lipid monolayers. This insertion was greatly enhanced by the neg. charged lipids 1,2-dioleoyl-sn-glycero-3-phosphoglycerol (DOPG) and E. coli cardiolipin. Insertion of SecA into these neg. charged lipids could be detected up to initial surface pressures of 34 mN/m for DOPG and 36 mN/m for E. coli cardiolipin, implying a possible role for neg. charged lipids in the insertion of SecA in biol. membranes. High salt concns. did not inhibit the SecA insertion into DOPG monolayers, suggesting not only an electrostatic but also a hydrophobic interaction of SecA with the lipid monolayer. ATP decreased both the insertion (factor 2) and binding (factor 3) of SecA to DOPG monolayers. ADP and phosphate gave a decrease in the SecA insertion to the same extent as ATP, but the binding of SecA was only slightly reduced. AMP-PNP and ATP-.gamma.-S did not have large effects on the insertion or on the building of SecA to DOPG monolayers. The physiol. significance of these results in protein translocation is discussed. Status: haveztSecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study Biochemistry314y 1119-1124yUtrecht 3584 CH, Neth. 813,&Breukink, E. Kusters, R. Dekruijff, B. 1992CHAPERONE CIRCULAR-DICHROISM COMPETENT STATE EXPORT LEADER PEPTIDE MALTOSE BINDING PROTEIN SECONDARY STRUCTURE TERTIARY STRUCTURE TRANSLOCATION TRIGGER FACTORInvitro Studies on the Folding Characteristics of the Escherichia-Coli Precursor Protein prePhoE - Evidence That SecB Prevents the Precursor from Aggregating by Forming a Functional Complex& European Journal of Biochemistry 208y2419-425 1 Sep 812.'Breukink, E. Kunsters, R. Dekruijff, B. 1993Invitro Studies on the Folding Characteristics of the Escherichia-Coli Precursor Protein prePhoE (European Journal Biochemistry, Vol 208, Pg 420, 1990)& European Journal of Biochemistry 2113 909 1 Feb 8110)Breukink, E. Keller, R.C.A. Dekruijff, B.  1993ESCHERICHIA-COLI LIPID PACKING MODEL MEMBRANE MODEL MEMBRANES PEPTIDES PHOSPHOLIPIDS PROTEIN TRANSLOCATION PROTEIN TRANSLOCATION ATPASE SECA VESICLE AGGREGATIONNucleotide and Negatively Charged Lipid-Dependent Vesicle Aggregation Caused by SecA - Evidence That SecA Contains Two Lipid-Binding Sites FEBS Letters 331 1-2h 19-24C 27 Sep Breukink, E. 1994]The Role of SecA and SecB in Protein Translocation Across the Escherichia coli Inner Membrane > N  University of Utrecht 1-98XQBreukink, E. Nouwen, N. van Raalte, A. Mizushima, S. Tommassen, J. de Kruijff, B. 1995PIThe C terminus of SecA is involved in both lipid binding and SecB bindingB&Journal of Biological Chemistry 27014 7902-7907 SSG82Brew, K. Castellino, F.J. Vanaman, T.C. Hill, R.L. 1970~:The complete amino acid sequences of bovine a-lactalbumin. , -  245( 4570-4582&Journal of Biological Chemistry. 816Breyer, R.M. Sauer, R.T. 1989leMutational analysis of the fine specificity of binding of monoclonal antibody 51F to lambda repressorl&Journal of Biological Chemistryo 264.22 13355-13360 5 Aug 815Breyer, R.M. Sauer, R.T. 1989leProduction and characterization of monoclonal antibodies to the N-terminal domain of lambda repressorl&Journal of Biological Chemistryi 264n22 13348-13354r 5 AugHABreyton, C. Haase, W. Rapoport, T.A. Khlbrandt, W. Collinson, I. 2002XQThree-dimentional structure of the bacterial protein-translocation complex SecYEG Nature 418662-665 HBBrickman, E.R. Oliver, D.B. Garwin, J.L. Kumamoto, C. Beckwith, J. 1984f`The use of extragenic suppressors to define genes involved in protein export in Escherichia coli$Molecular and General Genetics 1961H 24-27Boston, MA 02115, USA 817Z6/ESCHERICHIA EXPORT GENE PROTEIN SECA SUPPRESSORThe secA gene codes for a membrane component involved in protein export in E. coli. In order to define other genes whose products play such a role, extragenic suppressors of a secA(Ts) mutation were characterized. These suppressors fall into .gtoreq.3 genetic loci. One such locus is the prlA gene, previously identified by mutations which suppress signal sequence mutants. Thus, this approach may allow the identification of new genes involved in the export process.s 0026-8925Z[H\2YZ4-!WXVVUT S)R4 302$Bailey, C.J. Malthouse, J.P.G. 1991XQBINDING COMPLEXES ESCHERICHIA-COLI KINETICS L-SERINE MECHANISM SUBUNIT SYNTHETASECd]A Proton-Magnetic-Resonance Study of Hydrogen-Exchange Reactions of Yeast Tryptophan SynthaseEBiochemical JournalN 273E605-610S 1 FebYBaillet, B. Kohorn, B.D. 1996Hydrophobic core but not amino-terminal charged residues are required for translocation of an integral thylakoid membrane protein in vivo&Journal of Biological Chemistry` 27131 18375-18378 3042+Bailly, E. Bordes, N. Bornens, M. Klotz, C.s 1992ACTIN CENTROSOME COMPONENTS GAMMA-TUBULIN INTERMEDIATE FILAMENTS MICROFILAMENT MICROTUBULE MICROTUBULE-ASSOCIATED PROTEINS MITOTIC SPINDLE MONOCLONAL-ANTIBODY MYOGENESIS ORGANIZATION POLARITY XENOPUS EGGSjdA High Molecular Weight Centrosomal Protein of Mammalian Cells Is Antigenically Related to Myosin-II("Cell Motility and the Cytoskeleton232n122-132 3052+Bailly, E. Pines, J. Hunter, T. Bornens, M.f 1992ACTIVATED XENOPUS EGGS CDC2 PROTEIN-KINASE CELL FRACTIONATION CELL-CYCLE CENTROSOME CYCLE CONTROL CYCLIN LOCALIZATION FISSION YEAST M-PHASE MATURATION-PROMOTING FACTOR MESSENGER-RNA SACCHAROMYCES-CEREVISIAE SEA-URCHIN EGGS TYROSINE PHOSPHORYLATIONhCytoplasmic Accumulation of Cyclin-B1 in Human Cells -Association with a Detergent-Resistant Compartment and with the CentrosomeJournal of Cell Science 101529-5450 Mar 306Bains, G. Freire, E. 1991`YCalorimetric determination of cooperative interactions in high affinity binding processesRAnalytical BiochemistryS 1921 203-206  Jan` 307.(Bains, G. Lee, R.T. Lee, Y.C. Freire, E. 1992haMicrocalorimetric study of wheat germ agglutinin binding to N-acetylglucosamine and its oligomerst Biochemistry3150 12624-12628  22 Dec 30981Bairaktari, E. Mierke, D.F. Mammi, S. Peggion, E.d 1990>8ACIDS PROTEINS RESOLUTION SPECTROSCOPY WATER SUPPRESSIONConformations of Bombolitin-I and Bombolitin-III in Aqueous Solutions - Circular Dichroism, H-1 NMR, and Computer Simulation Studies Biochemistry2943 10097-10102 30 Oct 30881Bairaktari, E. Mierke, D.F. Mammi, S. Peggion, E.a 1990~ACIDS MASTOPARAN NUCLEAR MAGNETIC-RESONANCE PEPTIDES PROTEINS SECONDARY STRUCTURE SPECTRA SPECTROSCOPY VENOM WATER SUPPRESSIONConformational Studies by Circular Dichroism, H-1 NMR, and Computer Simulations of Bombolitin-I and Bombolitin-III in Aqueous Solution Containing Surfactant Micellesc Biochemistry2943 10090-10096N 30 Oct Bairoch, A. Boeckmann, B.  19910)The SWISS-PROT protein sequence data bankNucleic Acids Res.19Suppl: 2247-2249Bairoch, A. Apweiler, R. 2000PJThe SWISS-PROT protein sequence database and its supplement TrEMBL in 2000Nucleic Acids Research28 45-48 KSR  31160Bajorath, J. Kitson, D.H. Kraut, J. Hagler, A.T. 1991NGThe electrostatic potential of Escherichia coli dihydrofolate reductase111` 1-120*Proteins: Structure, Function and Genetics 310RKBajorath, J. Kitson, D.H. Fitzgerald, G. Andzelm, J. Kraut, J. Hagler, A.T.z 1991hbElectron redistribution on binding of a substrate to an enzyme: folate and dihydrofolate reductase93e217-224i0*Proteins: Structure, Function and Genetics 313d^Bajorath, J. Li, Z.Q. Fitzgerald, G. Kitson, D.H. Farnum, M. Fine, R.M. Kraut, J. Hagler, A.T. 1991jcChanges in the electron density of the cofactor NADPH on binding to E. coli dihydrofolate reductasei114263-2700*Proteins: Structure, Function and Genetics 312@9Bajorath, J. Kraut, J. Li, Z.Q. Kitson, D.H. Hagler, A.T. 1991piTheoretical studies on the dihydrofolate reductase mechanism: electronic polarization of bound substratesF8815 6423-64265 1 Aug6VOProceedings of the National Academy of Sciences of the United States of America >X SECRETORY sy sM s s s s)$ s s s s s s s s4 s7 s) s) s% s+X s'O s+i so s)2 s). s0 s0 s0 s0 s5 s5 s6  s6 s6 s7P s7] s7i s7k s7{ s7~ s7 s7 s7 s7 s7 s7 s7 s7 s7 s8* s8t s8w s8{ s8 s8 s s4txtiona8aa!aa1@'a2'a2'a5'a6M'a7'a8'a8'a8'a8i'aale$;ed?s Jooo)*oYorY>Y,d1d_dcdddgdhd6dddd d 2d)CdddMddd/C/A/A/A/A/A/A/A/A/A/A/A/A/A/A/A/A/A/A-A/A)A/A0AtAA"A#'A#&A#$A#%A-A0A.HA.=A/A0 AMA)A0A0A0A0A0A0A0A/ApA0A0A0#A0$A0'A0)A0*A08A0CA0UA0XA0XAX0AX0AX0AX0A1SsG)QI1I0I+ IzII0I,I0hI/:I1I0I'NI1(I1&I/ I1$I[I I$I/-I1I1I1I0II0II1)I1I0gI#I1I1!I0I)FI I1I/}I0IlI/I1"I)MI0I0I0I0I0I/I1I1I0I1 IXI0I*;I0I0I1I6h1p60I6I"I!oR1I0I+ IzII0I,I0hI/:I1I0I'NI1(I1&I/ I1$I[I I$I/-I1I1I1I0II0II1)I1I0gI#I1I1!I0I)FI I1I/}I0IlI/I1"I)MI0I0I0I0I0I/I1I1I0I1 IXI0I*;I0I0I1I"I!oRen YDeva(a)a&aVaZa a(a)Na)Oa*8a)@a#na&ra+Sa+]a&a+a,Ba,a,a-3a-:a-a-a-a-a.ka).a*a/6a(a/7a+a00a0a0a0a0a0a0a0a1a1a)0a0ala1a3a3 a3a3a46a4aa4ja4ra4a.Qa5a6a6!a63a6a6a7ha7ua8Ga8~a8a9a*Daa*a*=a zaaa"a,a-a-a.aa o( ￭(@((ʨ $    * !  翀IDE INTERCHANGE THIOL-DISULPHIDE EXCHANGEDissecting the Disulphide-Coupled Folding Pathway of Bovine Pancreatic Trypsin Inhibitor - Forming the First Disulphide Bonds in Analogues of the Reduced Protein5 2323e873-896 5 Aug-"Journal of Molecular Biology0*Darby, N.J. Freedman, R.B. Creighton, T.E. 1994ztDissecting the mechanism of protein disulphide isomerase: catalysis of disulphide bond formation in a model peptide. Biochemistry33 7937-7947 (` 3463Itakura, M. Iio, T. 1992BINDING CA2+-DEPENDENT MODULATOR PROTEIN CALCIUM CONFORMATIONAL CHANGE KINASE PEPTIDES SKELETAL-MUSCLE STOPPED-FLOW FLUORESCENCE TROPONIN-C TRYPTIC FRAGMENTSD=Static and Kinetic Studies of Calmodulin and Melittin ComplexJournal of Biochemistrye 112m2183-191s Aug8&Itikawa, H. Fujita, H. Wada, M. 1986rlHigh temperature induction of a stringent response in the dnaK(Ts) and dnaJ (Ts) mutants of Escherichia coliJournal of Biochemistry 996 1719-1724  3465 DNAJ 0021-924X 34660*Itikawa, H. Wada, M. Sekine, K. Fujita, H. 1989 DNAJ 0300-9084RPhosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase by the gene products of dnaK and dnaJ in Escherichia coli K-12 cells Biochimie71 9-10 1079-1087 34642+Itikawa, H. Mishina, Y. Wada, M. Fujita, H.c 1992DEPENDENT PROTEASE DNAK PROTEIN EXPRESSION HEAT-SHOCK RESPONSE INDUCTION PARTICIPATION PHOSPHORYLATION PRODUCTS SIGMA-32 SYNTHETASE Genetic Mapping and Biochemical Characterization of Suppressor Mutations sukA and sukB for a dnaK (Ts) Mutation of Escherichia coli K-12"Japanese Journal of Genetics671s 17-27 Feb 3467.'Itin, C. Burki, Y. Certa, U. Dobeli, H. 1993ACTIN ALDOLASE EXPRESSION GENES GLYCOLYSIS MALARIA CHEMOTHERAPY MUTAGENESIS PROTEIN RESOLUTION SELECTIVE INHIBITION SEQUENCE TUBULINzSelective Inhibition of Plasmodium-Falciparum Aldolase by a Tubulin Derived Peptide and Identification of the Binding Site,&Molecular and Biochemical Parasitology581135-143s Mar3 3469,%Ito, H. Hirano, A. Yen, S.H. Kato, S. 1991ALZHEIMERS-DISEASE AMYLOID AMYOTROPHIC LATERAL SCLEROSIS BETA-PROTEIN CENTRAL NERVOUS-SYSTEM ENTORHINAL CORTEX HIPPOCAMPUS NEUROFIBRILLARY TANGLES PARKINSONISM-DEMENTIA COMPLEX ON GUAM SENILE PLAQUES SPINAL CORDThis report concerns the immunohistochemical demonstration of beta-amyloid protein-containing neurofibrillary tangles (beta-NFTs) from patients with parkinsonism-dementia complex on Guam (PDC). Formalin-fixed paraffin-embedded tissue sections from the temporal lobe of nine PDC cases and the spinal cord of three were examined. An affinity-purified antibody to the N-terminal peptide sequence of beta-amyloid protein was used. beta-NFTs were demonstrated in the temporal lobes of the three oldest individuals. Some senile plaques, probably a manifestation of ageing, were also seen. The beta-NFTs were most frequent in the entorhinal cortex. Senile plaques were invariably present in the vicinity of the beta-NFTs. Conversely, in the regions without senile plaques, even though numerous neurofibrillary tangles were identifiable with the modified Bielschowsky method, no beta-NFTs were seen. The density of beta-NFTs appeared to be proportional to that of senile plaques, none was seen in cases lacking senile plaques. No beta-NFTs were detected in the spinal cords. Our data suggest that beta-NFTs result from secondary beta-amyloid deposition on certain neurofibrillary tangles.xqDemonstration of beta-Amyloid Protein-Containing Neurofibrillary Tangles in Parkinsonism-Dementia Complex on Guami.'Neuropathology and Applied Neurobiology 175^365-373i Oct&&&&&&&'''''''''''''y'yyyyyyy(((((((!!!!!!!!%!!!%%%%%%%%%- - - MMMMM)")")")")")")")")")")"ppppppppppp-j-j-j-j-j-j-jo-jooo22222222444444-n-n-n-n-n-n-n-n-n-n-nnnnnnnnnnnnn}}}}}}}},@,@}},@,@,@,@ooYYYYYYYWWWWWPPPPPPPPPPPRRRRRRRRRR$X$X$X$XhydrogenoI#I)I* IqIIIAI&III5I(I@I[I~I/IXIfIIIIIIII~IIwIIIIIIIIIIIII]IaIIIII ^I!I!-I!I!I"I"#I"pI#HI#I#I#I)I)I)I)Iert, P. Vigopelfrey, C. Esch, F. Lee, M. Dovey, H. Davis, D. Sinha, S. Schlossmacher, M. Whaley, J. Swindlehurst, C. McCormack, R. Wolfert, R. Selkoe, D. Lieberburg, I. Schenk, D. 1992D>AMYLOID PRECURSOR PROTEIN CELLS CLEAVAGE DISEASE GENE MUTATION^WIsolation and Quantification of Soluble Alzheimer's beta-Peptide from Biological Fluids Nature 359 6393325-327 24 Sep 7115Seubert, P. Oltersdorf, T. Lee, M.G. Barbour, R. Blomquist, C. Davis, D.L. Bryan,C-rA-sA-vA-|A-~A-A-A A-AAA'DA-A-A-A-A-A-A-A-A-A-A-A-A,A-A-A-A-A-A-A-A-A-A-A-A-A-A-A-A-A-A.A.A.A.A. A.A.A.A.A.+A.,A.0A.1A.1A1.A1.A.1A.1A.1A.1A.1A]1989v9999999}999 97989H9w99$9K99999994999=9V9U9W9u9v9~9}99999 9 F9 [9 ~9 9 9!9!9!9!9"9"Z9"[9"x9"w9#l9#9#9$9$79$D9$C9$V9$V9 36566-6?6666"6%666%6&6-6666/6J666 >6 ?666000 0!0$j00016233304448E555%6778893906666-6 9999 &9#e9+9,49-~9/.99?910742 15 NovVOProceedings of the National Academy of Sciences of the United States of AmericahXRQian, Y.Q. Otting, G. Furukubotokunaga, K. Affolter, M. Gehring, W.J. Wthrich, K. 6349Qian, W.L. Krimm, S. 19920*ABINITIO CONFORMATION DIMETHYL NORMAL MODEVibrational Studies of the Disulfide Group in Proteins .5. Correlation of SS Stretch Frequencies with the CCSS Dihedral Angle in Known Protein Disulfide Bridges Biopolymers324321-326 Apruf7mTok7n7u7777777777778888 ,1828<8C8F8L8U8X8_8c8e8h8t8v8888&<8888 999 )999999B9E9K9_9a9g909U 6-  &O-.)777778888 ,1828<8C8F8L8U8X8_8c8e8h8t8v8888&<888888  6-  &O-.)SxR*QPvO\,N.F@Bertelsen, E.B. Zhou, H. Lowry, D.F. Flynn, G.C. Dahlquist, F.W. 1999PITopology and dynamics of the 10 kDa C-terminal domain of DnaK in solutionProtein Science8343-354 jlf 5564-Bertozzi, C.R. Hoeprich, P.D. Bednarski, M.D.l 1992AMINO-ACIDS BOVINE SERUM-ALBUMIN CORRESPONDING C-GLYCOSIDES HELIX-FORMING TENDENCIES O-GLYCOPEPTIDES OVINE SUBMAXILLARY MUCIN PREFERRED CONFORMATION SOLID-PHASE SYNTHESIS STEREOSELECTIVE SYNTHESIS T-ANTIGEN STRUCTURESLFSynthesis of Carbon-Linked Glycopeptides as Stable Glycopeptide Models"Journal of Organic Chemistry5723 6092-6094 6 Nov,&Bertrand, R. Derancourt, J. Kassab, R. 1997Probing the hydrophobic interactions in the skeletal actomyosin subfragment 1 and its nucleotide complexes by zero-length cross-linking with a nickel-peptide chelatew Biochemistry36 9703-9714o JAH 55781Bertsch, U. Soli, J. Seetharam, R. Viitanen, P.V.e 1992BINDING ESCHERICHIA-COLI GENE-PRODUCTS GROEL IMPORT MOLECULAR CHAPERONE MOLECULAR CHAPERONES POLYPEPTIDE PROTEIN PROTEIN FOLDING PROTEIN IMPORT PURIFICATION RIBULOSE BISPHOSPHATE CARBOXYLASE STRESS PROTEINS0*Chloroplasts of higher plants contain a nuclear-encoded protein that is a functional homolog of the Escherichia coli chaperonin 10 (cpn10; also known as groES). In pea (Pisum sativum), chloroplast cpn10 was identified by its ability to (i) assist bacterial chaperonin 60 (cpn60; also known as groEL) in the ATP-dependent refolding of chemically denatured ribulose-1,5-bisphosphate carboxylase and (ii) form a stable complex with bacterial cpn60 in the presence of Mg.ATP. The subunit size of the pea protein is almost-equal-to 24 kDA-about twice the size of bacterial cpn10. A cDNA encoding a spinach (Spinacea oleracea) chloroplast cpn10 was isolated, sequenced, and expressed in vitro. The spinach protein is synthesized as a higher molecular mass precursor and has a typical chloroplast transit peptide. Surprisingly, however, attached to the transit peptide is a single protein, comprised of two distinct cpn10 molecules in tandem. Moreover, both halves of this ''double'' cpn10 are highly conserved at a number of residues that are present in all cpn10s that have been examined. Upon import into chloroplasts the spinach cpn10 precursor is processed to its mature form of almost-equal-to 24 kDa. N-terminal amino acid sequence analysis reveals that the mature pea and spinach cpn10 are identical at 13 of 21 residues.Identification, Characterization, and DNA Sequence of a Functional Double groES-Like Chaperonin from Chloroplasts of Higher Plants8918 8696-8700 15 SepVOProceedings of the National Academy of Sciences of the United States of America  558LEBerzalherranz, A. Joseph, S. Chowrira, B.M. Butcher, S.E. Burke, J.M. 1993ztBINDING CATALYTIC RNA CLEAVAGE INVITRO INVITRO SELECTION REQUIREMENT RIBOZYME RNA STRUCTURE SATELLITE RNA SITE VIRUS^WEssential Nucleotide Sequences and Secondary Structure Elements of the Hairpin Ribozymeh EMBO Journal126 2567-2574 Junu 560$Beschiaschvili, G. Seelig, J.i 1990ADSORPTION DIFFERENTIAL SCANNING CALORIMETRY HYDROPHOBICITY INTERFACE MEMBRANES MONOLAYERS NUCLEAR MAGNETIC-RESONANCE PENTAGASTRIN-RELATED PENTAPEPTIDES TRANSBILAYER HELICES TRYPTOPHANpjPeptide Binding to Lipid Bilayers - Binding Isotherms and zeta-Potential of a Cyclic Somatostatin Analogue Biochemistry2949 10995-11000e 11 Dec 559(!Beschiaschvili, G. Baeuerle, H.D.. 1991VO1-PALMITOYL-2-OLEOYLPHOSPHATIDYLCHOLINE VESICLE BILAYER-MEMBRANES BINDING CD ELECTROPHORETIC MOBILITY ELECTROSTATIC EFFECT ELECTROSTATIC POTENTIALS ADJACENT HUMAN-ERYTHROCYTES LARGE DIVALENT-CATIONS LARGE-LIGAND ADSORPTION MELITTIN MODEL MEMBRANES NMR, P-31 PHOSPHATIDYLCHOLINE MEMBRANES PHOSPHOLIPIDS POTENTIAL CHANGE SELF-ASSOCIATIONuF@Effective Charge of Melittin upon Interaction with POPC Vesicles$Biochimica et Biophysica ActaI 10682195-200 30 Sep 561$Beschiaschvili, G. Seelig, J.i 1992ANTAGONISTS CYCLIC SOMATOSTATIN ANALOG DIMYRISTOYLPHOSPHATIDYLCHOLINE MELITTIN PHOSPHATIDYLCHOLINE MEMBRANES SUBSTANCE-P THERMODYNAMICS VESICLEShbPeptide Binding to Lipid Bilayers - Nonclassical Hydrophobic Effect and Membrane-Induced pK Shifts Biochemistry3141 10044-10053  20 Oct,+ Stability,, z+ z,0 z+ z,7 z z{ z,= z,G z z,a z,g z,l z,r z,t z,v z z zR z. z9 z, z3 z> zX z z, z z C z z= z F z z  zZ z  z-. z-< z- z- z- z- z, z- z. z.  z.! z." z.S z.W z.` z H z, z. z. z- z. z z. z. z. z. z1QUery1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s1s.F.1/1/1/1/%1/&1/(1/)1/*1)"1s1/D1/E1/_1/v1/S1- 1.1-11/1/1/1/1/1/1/1/1/1/1/1/1/111111-1-1/101.H10101/1.410I10P10Q10Y10Z1-110r10t1010101010101011HTbin1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L1L2L2L2L2L2L2L2L2L2L2 L2 L2 L2 L2 L2L2L2L2L2L2L2L2L2L2L2L2L2L2L2!L2 L2"L2$L2%L2)L2(L2(L2(L2(L2(L2(L2(L5555,5,,KKKKKKK========$==$==========        &&RRRRRRR%%%%%%UUUUUUUUUUU J J J J J J J J Jwwwwwwwwoooooooo&&&&&&"""""""""""NNNNNNNNNN\\\\\\\\\\\RRRRRRxxxxx,,,,,,,,,,,IIIIIIIIIIIIIIIII'U'UAAAAAA{{{{{{{((((((((((XXXXXXLLLLLLLLLLLLLLL#####OOOOOOOOOOO))))) structures u u( u` um u" u u u u u u u uh u uY u u u 6 u  u  u! u! u! u"" u"7 u"? u"R u"T u"e u"i u"p u"~ u" u" u# u# u# u$D u$ u$ u%E u%P u% u&U u&Y u& u)5 u+ u% u+ u  u+ u* u+ u+ u+@ u* u  u+ u, u ur3And3e3 e3 e3e3e3e3e3#e3e3+e3-e3.e30e31e33e39e37e3?e3De3Ie3Oe3Qe3ce3[e3We3ge3he3re3me3se3ue3ne3xe3je3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e3e-e[e eee$e,e3e3e Abundance c c*k c c( c2 c ct c  tt t t t t#{ t+s t8 tet 8s&ss)ss6s6s6s7s85ssoudt6ftsmzymesca6666#6+y6+65666))61q'62|'62'62'64g'64}'65D'65_'65w'65u'66'66'66'666'66K'66m'66'67'67'68H'68Q'68n'68t'68'66c#ade&7e1Se1ie1oe1qe1e1e1e2e2e2 e24e2Le2Ze2Ye2ae2be2ee2ge2ge2ge2ge2gez971;168%377014 8!80535'79#1579882aA210a)68a8bbadi!ilityYkevich!)normal out!Grahamqsence(oluterptiveT#&TRACT$Gu!undance$cad!$eemy n DnnnKnnnPnn)nT nthamoeba)cepting ssibility ompanYing retion* umulationratei ETYLcholine NEURAMINICi 2id iii@ii Yi%ii"i i Wii\iar Dichroism Disulfides/*chemistry Enzyme Stability/genetics Guanidine/chemistry Human Kinetics Models, Chemical Muramidase/*chemistry/genetics Mutagenesis, Site-Directed Protein Denaturation/genetics *Protein Folding Protein Structure, Secondary/genetics Protein Structure, Tertiary/genetics Spectrometry, Fluorescence Spectrophotometry, Ultraviolet Structure-Activity Relationship Support, Non-U.S. Gov'tSJE JAHe\Vhttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://dx.doi.org/10.1021/bi9921945_^8]\[ZYX 6544,%Riggs, P.D. Derman, A.I. Beckwith, J. 1988>8ESCHERICHIA FUSION GENE LACZ PROTEIN SECA SECE SECRETIONThe secA gene of Escherichia coli is derepressed in cells that have a defect in protein export. It is demonstrated that the .beta.-galactosidase produced by a secA-lacZ gene fusion strain is regulated in the same way. Studies on the fusion strain reveal that the promoter or a site involved in regulation of the secA gene is located considerably upstream from the structural gene. The properties of the fusion strain provide a new selection for mutants that are defective in protein export. Selection for increased lac expression of a secA-lacZ fusion strain yields mutations in 3 of the known sec genes, secA, secD, and prlA/secY. In addn., mutations in several genes not previously known to affect secA expression were obtained. A mutation in 1 of these genes causes a pleiotropic defect in protein export and a cold-sensitive growth defect; this gene, which maps at .apprx.90 min on the bacterial chromosome, has been named secE. 0016-6731VPA mutation affecting the regulation of a secA-lacZ fusion defines a new sec geneGenetics 1184s571-579Boston, MA 02115, USA- 6545Bc/Fc/Hc/Mc/Nc/[c/gc/kc/oc/pc/tc/wc/xc/Zc/Xc/Sc.c/c/{c.ic,bc. c.c.c.c-c/0c/c/c.c/c/c/cEcc)c+3c(c)c(c+c-Pcc+Ycc/c/c/c/c/c/c` 2735"4 67 88 959696979)9'Z99"M4 40P20P8465)555 D5'55#5555"5%5&5p505755&5U55?5(0(00(0)0-0-0.0.0/60/0000+00>00G00P00i00000000000/0/:01p01r01{01020202020202030(06)0707Y070508p0*0/0000000001p01r01{01020202020202030 0 1 2 3 4 5 6 kingt'k'k Ek ddddddd>dddFdtdsdudvd!dd&ddd d!d!d%d%d&wd*d,Hd-Qd/dd0d0d1Jd2'2'2'2'3<'3'4'5\'7'7'7!'7*'7;'7<'8'8'9>'h'4 '7'4''7D''7E''1?''sd3'd-| doms'k Ek ddddddd>dddFdtdsdudvd!dd&ddd d!d!d%d%d&wd*d,Hd-Qd/dd0d0d1Jd2'2'2'2'3<'3'4'5\'7'7'7!'7*'7;'7<'8'h'4 '7'4''7D''7E''1?''sd3'd-| domsj~|}, A.L. Aswad ВPW.29 Aimo Х 0 øAswad, D.W.A Х Х  ø Aizawa Х1 # Aizawa19922% Aizawa19929= Ajioka19955% Akagi1990 Akamizu1992!o Akasaka1991!n Akasaka1991# Akasaka1992!p Akasaka1992" Akasaki1993)Akasako-Furukawa1998  Akashi1994i Akerfeld 5425<5Nadler, S.G. Tepper, M.A. Schacter, B. Mazzucco, C.E. 199215-DEOXYSPERGUALIN CELLS CYCLOPHILIN CYCLOSPORIN-A CYTOSOLIC BINDING-PROTEIN EXPRESSION INVITRO LYMPHOCYTES PEPTIDYL-PROLYL ISOMERASE RECEPTORtmInteraction of the Immunosuppressant Deoxyspergualin with a Member of the Hsp70 Family of Heat Shock ProteinsDScience 258n 5081484-486 16 Oct 5424>7Nadler, S.G. Kapouch, J.L. Elliott, J.I. Williams, K.R. 1992|DESIGN DNA-BINDING EPSILON ESCHERICHIA-COLI GENE IDENTIFICATION LIGANDS MESSENGER-RNA PROTEIN CONFORMATION RIBONUCLEOPROTEINShuffling of Amino Acid Sequence - An Important Control in Synthetic Peptide Studies of Nucleic Acid-Binding Domains - Binding Properties of Fragments of a Conserved Eukaryotic RNA Binding Motif&Journal of Biological Chemistry. 2676 3750-3757 25 Feb 5426("Nagadome, H. Kawano, K. Terada, Y. 1993\UADSORPTION HYDROGEN-EXCHANGE HYDROXYAPATITE LYSOZYME NMR PANCREATIC TRYPSIN-INHIBITORTThe lysozyme-hydroxyapatite interaction was studied by measuring individual hydrogen-deuterium (H-D) exchange rates of amide protons. The H-D exchange reaction was initiated by transferring the lysozyme adsorbed on hydroxyapatite powder from H2O into D2O. After various H-D exchange time periods (pH 7.0, 25-degrees-C), the complex was dissociated and the remaining hydrogen label was determined by 2D NMR analysis. The H-D exchange rate of amide protons of residues 9,11, 13, and 83 was slowed in the hydroxyapatite-lysozyme complex compared with free lysozyme. Residues 9, 11 and 13 positioned at the back of the active site would be the location of the binding site.ztIdentification of the Adsorbing Site of Lysozyme Onto the Hydroxyapatite Surface Using Hydrogen Exchange and H-1 NMR FEBS Letters 317t 1-2 128-130 8 Feb 5427D=Nagahari, K. Kanaya, S. Munakata, K. Aoyagi, Y. Mizushima, S.g 1985^WBETA CLONING ENDORPHIN ESCHERICHIA EXPORT FUSION GENE HUMAN OMPF PROTEIN SECA TRANSPORTThe ompF gene codes for a major outer membrane protein of E. coli. A plasmid was constructed in which the structural gene for human .beta.-endorphin [61214-51-5] is preceded by the upstream region of the ompF gene consisting of the promoter region and the coding regions for the signal peptide and the N terminus of the OmpF protein. When the plasmid was introduced into E. coli N99, an OmpF-.beta.-endorphin fused peptide was synthesized and secreted into the culture medium through both the cytoplasmic and outer membranes. The OmpF signal peptide was cleaved correctly during the secretion, indicating that the export of the fused protein across the cytoplasmic membrane was dependent on the signal peptide. The secretion into the culture medium was apparently selective. Neither .beta.-lactamase nor alk. phosphatase (both are periplasmic proteins) appeared in the culture medium in significant amts. The mode of passage of the fused peptide across the outer membrane is discussed. 0261-4189Secretion into the culture medium of a foreign gene product from Escherichia coli: use of the ompF gene for secretion of human .beta.-endorphin  EMBO Journal4 13Al 3589-3592lKanagawa 227, Japan9 5428>8Nagahora, H. Ishikawa, K. Niwa, Y. Muraki, M. Jigami, Y. 1992pjBARLEY LECTIN EVOLUTION GENES HUMAN LYSOZYME ISOLECTIN PROPEPTIDE PROTEIN RESOLUTION SIGNAL-SEQUENCE YEASTTMExpression and Secretion of Wheat Germ Agglutinin by Saccharomyces-Cerevisiae& European Journal of Biochemistry 2103989-997 15 Dec2Inm2c2c2c/$c/ c2c2c2c2c2c2c2c2c2c2c2c2c2c tc2c2c2c2c2c2c2c2c2c2c2c2c2c,c3c3c3c3c3c3c3c3c3"c3#c3'c3)c3*c3,c3.c30c31c32c33c35c3:c37c3@c3<c3>c3Gc3Hc3Jc3c3QcN277)0)0%A0)0)0)0,C0)0)0+Y00000101)010101010202020202020303030303:03`03_03^03]03\030304040404C04]04\04[04p04w04y04z04{04|040401204)04s05a05`05_05050606a07)07|0808c08g08l08m08t08w08|08~09e0,01010202020202030303:03`03_03^03]03\03030120 07/'870'971'972'96`'9!{1 2+j01;'21W'22'22R2R2R2R2R2R2R2R2R2R2R2RRRIRHRZRYR\RbR @ 64b47 298  5602 2002 Dec 20HBStructure of the LDL receptor extracellula 6705LFRudensky, A.Y. Prestonhurlburt, P. Hong, S.C. Barlow, A. Janeway, C.A. 1991ANTIGEN-BINDING SITE CHAIN CLONES COMPLEX HISTOCOMPATIBILITY MOLECULES IA MONOCLONAL-ANTIBODIES RESTRICTION SPECIFICITY T-CELL RECOGNITIONCD4 T cells recognize peptide fragments of foreign proteins bound to self class II molecules of the major histocompatibility complex (MHC). Naturally processed peptide fragments bound to MHC class II molecules are peptides of 13-17 amino acids which appear to be precessively truncated from the carboxy terminus, perhaps after binding to the MHC class II molecule. The finding of predominant self peptides has interesting implications for antigen processing and self-non-self discrimination. D=Sequence Analysis of Peptides Bound to MHC Class-II Moleculesl Nature 353 6345622-627l 17 Oct9145101445 1997 Mayr6/Interaction of Hsp70 chaperones with substratess 342-9SDetermination of the structure of the substrate binding domain of the Escherichia coli Hsp70 chaperone, DnaK, and the biochemical characterisation of the motif it recognizes within substrates provide insights into the principles governing Hsp70 interaction with polypeptide chains. DnaK recognizes extended peptide strands composed of up to five consecutive hydrophobic residues within and positively charged residues outside the substrate binding cavity.'HAZentrum fur Molekulare Biologie, Universitat Heidelberg, Germany.*$Rudiger, S. Buchberger, A. Bukau, B.@:97290444 1072-8368 Journal Article Review Review, TutorialNat Struct BiolBinding Sites Escherichia coli/chemistry Heat-Shock Proteins 70/*chemistry Models, Molecular Oligopeptides/chemistry *Protein Conformation Substrate Specificity Support, Non-U.S. Gov'tjdhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9145101~@MEAnss cs:sss(sss ps s ssAs|sss0s?sfss S s?sxss4s7s"4s"s&s&ss,s52s5s6&s63s7Gs7ds7rs7s8 s8s8Is8hs8s8ssurable eddd0d3d4d dkd dyddd Yd&_d0d6}d7/d7md7d8rd8dHdmgm @mmmmRO Refolding s s s s r r!D r#z s% s% s#L s4) s5 s6 s6) s69 s6< s6G s6K s6W s6 s6 s6 s6 s7 s7 s7# s7- s73 s7< s7A s7D s7X s7 s7 s7 s7 s82 s8t s!D s!D r-usrmation7ractile7 s7$orysg g6ggPgUg g ig|g}gggggggggg \g"xg# g$g$g$g$g$g220012222221V22222221>2222222222222323623l23r23m23q23w23s23p23|23}23~23232323232323232323232323232323232323232324#24242424242123i242124222424242&Ofc&N&N&N&N&N&N'N'N'N'N'!N'"N'$N'%N'&N+HN+KN+LN+MN+NN+ON+TN+UN+VN)5N)(N)+N),N)-N)3N)1N))N) N)#N)*N+XN+\N+JN+]N+N+N+^NNrNuNNNNNNNNNNNNNNNNNNN6 recombinant6 t6 t7 t7! t7" t7, t7- t7> t7C t7E t7G t7H t7I t7h t7n t7v t7w t7~ t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t8 t8 t8 t6 t8K t8P t8X t8c t8f t8h t8i t8v t8 t8 t8 t8 t" t t7 t t t Sj S> S Sj S S S! S% S&O S&_ S S'Q S6 S6 S7 S7" S7< S7C S7G S7v S7 S7 S88 S8v S8 S8 S? S tiona  a[ a. a a a a t7 t7 t7 t7 t7 t" t t7 t t t Sj S> S Sj S S S! S% SO& S_& S SQ' S6 S6 S7 S"7 S<7 SC7 SG7 Sv7 S7 S7 S? S tiona  a[ a. a a responses sss)ssss^s]ssss'sss#^s%s+qs0s0s#s4)s6 s6as6s6s7:s7Cs7Is7as7ds7}s7s7s7s8@s8Js8Ls8s8sKs i7 i ` i  i D i  i i i i i i i i+ i5 i#s i i i i i" iF i i" i i i7 i  i i' i# i% i)% i+| i+} i7e i7 i8< iiblet t VP vo vT vU v v4 vBILAYER-MEMBRANES CA-2+-INDUCED FUSION FUSOGENIC CAPACITIES ION BINDING KINETICS MEMBRANE-FUSION MODULATION MONO-VALENT PHASE-CHANGES VESICLESDivalent Cation-Induced Lipid Mixing Between Phosphatidylserine Liposomes Studied by Stopped-Flow Fluorescence Measurements - Effects of Tempe"^3"o1"1"1"1"1"1"1"1"1"1"1#1#1#1#1# 1)1#91#N1#W1#`1#p1#{1#1#1#1#1#1#1#1#1#1#1#1#1#1#1#1#1#1$1$ 1$ 1$1$1$"1$(1$.1$01$K1$O1$^1$]1$\1$a1$b1$s1$t1${1$~1$~1$~1$~1 Ashtonrickardt1993# Ashwell1993+ Askin1998 Aslanidis1990 Assa1986vAssamunt1993 ~Asseline1993 Assmann1993 Ataka1990i Atassi19789 Atassi19900 Atassi1992  Atassi1992  Atassi1992  Atassi1992  Atencio1992 Atherton19922" Atkins19909 Atkins19919 Atkins19911 Atkins1993 ' Atkins19944 Atkins19944 Atkins1995 Atkinson1994/*/&8"8h3 *<*'5Nv 926:3Bushfield, M. Savage, A. Morris, N.J. Houslay, M.D. 1993BINDING-SITES DIABETES-MELLITUS GLUCAGON RECEPTOR GLYCOGEN PHOSPHORYLASE INSULIN RESISTANCE ISLET AMYLOID POLYPEPTIDE LIVER PLASMA-MEMBRANES PEPTIDE RECEPTORS RAT-LIVER SKELETAL-MUSCLEA Mnemonical or Negative-co-operativity Model for the Activation of Adenylate Cyclase by a Common G-Protein-Coupled Calcitonin-Gene-Related Neuropeptide (CGRP)/Amylin Receptor1Biochemical Journal5 293l229-2369 1 Jul2,Bushueva, T. L. Busel, E. P. Burstein, E. A. 1980rkSome regularities of dynamic accessibility of buried fluorescent residues to external quenchers in proteinsoArch Biochem Biophys 204E1r 161-6. Oct 1B7425635s JAHpjdhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=7425635 927F?Bushueva, T.L. Uroshevich, O.I. Teplova, M.E. Tonevitskii, A.G.i 1992d]Interaction of the Toxic Plant Protein Ricin with Model Membranes - A Study with FluorescenceCMolecular BiologyT263P474-480RMay-Jun  928&Bushweller, J.H. Bartlett, P.A.o 1991A ALPHA CHAIN ENHANCEMENT MEASUREMENTS FIBRINOGEN-LIKE PEPTIDES HERPES-SIMPLEX VIRUS MAGNETIC-RESONANCE NMR-SPECTROSCOPY PORCINE PANCREATIC ELASTASE ROTATING-FRAME SYNTHETIC PEPTIDES X-RAY CRYSTALLOGRAPHYInvestigation of an Octapeptide Inhibitor of Escherichia-Coli Ribonucleotide Reductase by Transferred Nuclear Overhauser Effect Spectroscopy Biochemistry3033 8144-81513 20 Aug.'Bustamante, C. Rivetti, C. Keller, D.J. 199760Scaning force microscopy under aqueous solutions,%Current Opinion in Structural Biology@7 50709-716,%Butcher, S. Dieckmann, T. Feignon, J. 1997:3Solution structure of a GAAA tetraloop receptor RNA  EMBO Journal1624 7490-7499 929"Butenhof, K.J. Gerken, T.A.r 1993CLONING CONFORMATIONAL-ANALYSIS FORCE-FIELD GLYCOSYLATION MUCOUS GLYCOPROTEINS O-LINKED GLYCOPROTEINS OVINE SUBMAXILLARY MUCIN PROTEINS RANGE SEQUENCEStructure and Dynamics of Mucin-Like Glycopeptides -Examination of Peptide Chain Expansion and Peptide-Carbohydrate Interactions by Stochastic Dynamics Simulations Biochemistry3210 2650-2663 16 Mar 930@:Butrynski, J.E. Jones, T.L.Z. Backlund, P.S. Spiegel, A.M. 1992BETA-GAMMA BOVINE BRAIN GAMMA-SUBUNIT GTP-BINDING IDENTIFICATION METHYL-ESTER NUCLEOTIDE BINDING PROTEINS P21RAS RAS PROTEINS SIGNAL TRANSDUCTIONuDifferential Isoprenylation of Carboxy-Terminal Mutants of an Inhibitory G-Protein alpha-Subunit -Neither Farnesylation Nor Geranylgeranylation Is Sufficient for Membrane Attachmentc Biochemistry3134 8030-80354 1 Sep0*Butterfield, S.M. Patel, P.R. Waters, M.L. 2002~:Contribution of aromatic interactions to a-helix stability)*.(Journal of the American Chemical Society 124 9751-9755 JAH>8Buttner, K. Blondelle, S.E. Ostresh, J.M. Houghten, R.A. 1992PIPerturbation of peptide conformations induced in anisotropic environments  Biopolymers 326575-583 Jund 931^AMINO-ACIDS ENERGY MEMBRANES PARAMETERS PERFORMANCE LIQUID-CHROMATOGRAPHY PREDICTION PROTEINS RESIDUES RETENTION COEFFICIENTS TIMES 932b\Buxbaum, J.D. Oishi, M. Chen, H.I. Pinkaskramarski, R. Jaffe, E.A. Gandy, S.E. Greengard, P. 1992CDNA CULTURE DEMENTIA DISEASE HUMAN-ENDOTHELIAL CELLS IDENTIFICATION INHIBITOR LOCALIZATION MESSENGER-RNA PEPTIDE PHOSPHORYLATION PROTEIN-KINASE PROTEIN-PHOSPHORYLATION PROTEOLYSIS{Cholinergic Agonists and Interleukin-1 Regulate Processing and Secretion of the Alzheimer beta/A4 Amyloid Protein Precursora8921 10075-10078o 1 Nov0VOProceedings of the National Academy of Sciences of the United States of AmericahBuxbaum, J. N. 2003_Diseases of protein conformation: what do in vitro experiments tells us about in vivo diseases? * 3 N U Trends Biochem Sci2811585-592.'Bychkova, V.E. Pain, R.H. Ptitsyn, O.B. 1988`YThe 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Letters 238d2231-234  10 Oct 934 JCBychkova, V.A. Berni, R. Rossi, G.L. Kutyshenko, V.P. Ptitsyn, O.B. 1992HARetinol-binding protein is in the molten globule state at low pH. Biochemistry31 7566-7571 SJE-"Bychkova, V.E. Ptitsyn, O.B. 1993.'The molten globule in vitro and in vivon6/Chemtracts - Biochemistry and Molecular Biology4133-163 JAHLFBychkova, V.E. Dujsekina, A.E. Fantuzzi, A. Ptitsyn, O.B. Rossi, G.-L. 1998ZSRelease of retinol and denaturation of its plasma carrier, retinol-binding protein.Folding and Design3 285-291 SJELEBycroft, M. Matouschek, A. Kellis, J.Y., Jr. Serrano, L. Fersht, A.R.o 1990PJDetection and characterization of a folding intermediate in barnase by NMR Nature 346t488-490 JAHDunlap. C.A. Tsai, M.-D. 2002bUse of 2-aminopurine and tryptophan fluorescence as probes in kinetic analyses of DNA polymerase b a  Biochemistry41 11226-11235 JAH4-Cabelli, R.J. Chen, L. Tai, P.C. Oliver, D.B.I 1988[SecA protein is required for secretory protein translocation into E. coli membrane vesiclesBI Cell554683-692c Stony Brook, NY 11794, USA 943n60ESCHERICHIA PROTEIN SECA SECRETORY TRANSLOCATIONPIThe sol. and membrane components of an Escherichia coli in vitro protein translocation system prepd. from a secA amber mutant, secA13[AM], contain reduced levels of SecA and are markedly defective in both the cotranslational and post-translational translocation of OmpA and alk. phosphatase into membrane vesicles. Moreover, the removal of SecA from sol. components prepd. from a wild-type strain by passage through an anti-SecA antibody column similarly abolishes protein translocation. Translocation activity is completely restored by addn. of submicrogram amts. of purified SecA protein, implying that the obsd. defects are solely related to loss of SecA function. The translocation defect can by overcome by reconstitution of SecA into SecA-depleted membranes, suggesting that SecA is an essential, membrane-assocd. translocation factor. 0092-8674 SSGJAHn nnnNn-.n-/n-0n-1n-2n-3n-4n,n,n-Rn,n*n-Sn,n,n,n-Nn-;n-Tn-Un-Vn-Wn-Xn-Yn-Zn-rn-sn-tn-un-vn-xn-yn+n n ,nn n}nn$ln'Dnncn=n^nnn-n-n-n-n-n-n-n-n-n-n-nARDizkatbtabilitys [len"GENESES( is n n n n n n. n3 ni n nt n n/ n7 n n n n n < n = n A n @ n  n  n  n)* n C n  n / n  n0 nM nQ n n n n n n# n n n n n n n[ n( n ny nd0@"tJ"ua"va"x/Naturel/u/u/u-u.Hu0u0u/u0 u0)u-u0su0wu0u0u0u0u0u0u0u0u#u)u1u0uu@u=u2u[u u1u1u/u2u"u2^u2u2u2u2u3 u3u3"u3(u3Qu-u3u3u4u4%u4du4cu49u"u1u)u)uu1u2u4u)u20ulu4u)u)u)u+u2u59u5Su5su5ru5u5u6+u6.u63u6Au6Tu6u6u6u6u6u6u6u6u6u6u6u6u6u6u6u6u7u7u7u7u7u7'u7,u7]u7u7u83u8?u8{u8u8u8u8u8u8u8u8u8u9=u!|uzu u u]JTRendsnwp Gp p Wp p p p p 2p >p Np ,p p p #p $p*Qp p pppBpCpFpWpop{pppppppBpJp*)p1p0ppTpQppprpwpppp p#p0p p!p#t#et$t$t$t$t$t%t%t,YByt,`C)C,eC&C&C,xC,C,C,C,C,C,CCC,C,C,C,C,C,CC(C-&CC C'CC C*mC,C!9C-+C&}CnCCCCC(C*C)C!:C$C,TC%kC-CCC-4C->C-DC-EC-FC-KC,C-XC-XC-XC-XCX-C-XC-XC-XC4(4dT@LDL8(8(H$,P@8L0X88PȀ\Lh Āx(|LPph,h̀(th܀tˆHЀ0|t((Ơ@d|6Gov't6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a $ PARtially%B c&! c, c* c* c cc c. c- c. c.9 c c. c( c( c/ c#' c#& c0" c* c0 c0 c1 c/ c0 c2` c3: c3` c3 c3 c4G c4 c  c6 c6 c7< c8 cu cG c% c0 c" c c  c6 c cv c c_ c c"y c) c#{ c# c+o c+} c5 c6 c6 c6< c6D c6n c6} c64State68s6<s6>s6?s6@s6Bs6Cs6Es6Gs6Hs6Is6Js6Ns6Ss6Zs6]s6`s6ns6ts6{s6}s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s7s7s7s7s7s7 s7!s7*s79s7;s7<s7Bs7Ds7Ks7Ps7Xs7^s7`s7ds7ds7ds7ds7ds showt&e e eEeeXeweee#eXeeeheeeeMeOeaeeeeee;e<ee e eMeRee)eee^eeeCe _e!e"Ee"ye#qe$|e&0e)(e+aee)Deeee#Le,e+Yc#c0c0c1c0cUCLEOTIDE-SEQUENCE CYTOCHROME P-450 REDUCTASE GAP JUNCTION PROTEIN INTEGRAL MEMBRANE-PROTEINS LIGHT-HARVESTING POLYPEPTIDES MEMBRANE-PROTEINS NICOTINIC ACETYLCHOLINE-RECEPTOR OPTIMIZATION PHOTOSYNTHETIC REACTION CENTER RAT-LIVER CYTOCHROME-P-450 RHODOBACTER-SPHAEROIDES R-26 SEQUENCE-ANALYSIS STRUCTURE PREDICTION0xqQuadratic Minimization of Predictors for Protein Secondary Structure - Application to Transmembrane alpha-Helices 23212165-191 5 Jul"Journal of Molecular BiologyL SyNthetic T) TE T T T T T T T T T T% T` T Tm T T T T T T  T  T! 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T=" Te" Tz" T# T1# Ta# T# T# T:$ Tt$ T$ T$ T% T% T% T*& Tf& Tr& Tz& T  T T- T T;/ T/ Ty0 T T T T T TFunctionj,apa'^a2aXa`acaaaaa/aasa#a0a*aaaaaaa1aeaaaa_aaaaSaaa a a a a a!a"a"[a"^a"a"a#Ja#Sa#Va#ia#a#a#a$$a$=a$Fa$a%a%a%a%a%a^ #NIDULANSeee xe e"e$?e$See(eba"Xlingooercendenrerkamp' lse6}eenrr{rrm+^mtm.m1.m2m3m+mann(r r.$z.%r6Unhaus'#radko haus3 m6m9Dmmannt'Utlispach/ o8n oogg)g\v^v_v:vvvMssssotelov8G'uwevadww wiarowska i1991 d Hicke1990 Hicke1991* Hicke1997* Hicke1998 Hickey19929Z Hickey19922 Hicks1992 e Hicks1993* Hicks1996 Hideg1993 f Hider1988# Hider1993% Higashijima1992# Higashijima1992  Higashijima1992U Higashino1993H Higgins1991 Higgins1992"f Higgins1992 g Higgins1992 Higgins19| Unfolding,1 rO r r r+ r+E r,F r,I r,a r r, r, r, r r-" r-# rF r  r" r- r, r-  r( r r[ r-> r-S r- r- r- r- r- r- r- r- r- r- r- r r.\ r./ r+D r. r. r. r. r.: r. r r r r/2 r/g r/ r+ r+ r+ r+ r+ r/ r/ r/ r#O$$O$=O$FO$O%O%O%O%O)O&O&O&O&rO&ONO++O,O,6O)O*sO,KO,PO,QO,RO&<O-O UOO O$O-O-O-O.O.O.OO-O-OEOO(O/OKOsOO)O"^O"uO"O"O"O"O#O*sO##OKOtOsOrOO)Oally  MODULARt6t6t7,t7ot7t8@t8pt8t8ity{tedQd@dXdTd!d Rd0dd6"d7d7d8]dd)  i  s s s+ sp s8S s! sp s6" s6 s6 s7. s7h s7t s6 s8 s) s if i i i*A i. i0 i2 i3 i5 i  i i% i6 i7. i7 iing4 o o oj o% o8 o  o g o"M o'P o67 o68 o8 oone e e  e e j e  e e> e e es e e en e e e e e# e, eaa a a&Baaaallyr  r  r  rS r r r) r-M r  rropic s( Y Y* Y$ Y$: Yl YYPEYPEr  r  rS  ` Lazdunski1991  Lazdunski1992  Lazdunski1992$ Lazdunski1992.Lazowska1993' Lazure199392 Lssle1997  Le19919 Le1992 Le1993( Le19949) Le199511 Le20022Le Blanc1991/ le Coutre2000 Le Du19928 Le Duff2003( Le Guerneve1996Le Motte19942.Le Motte1999m4`Le Trong2002 Leach1992k Leach1993! 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Sugai1993$ Sugai1993,` Sugai19960 Sugai1997* Sugai1998,s Sugai1998- Sugai19992B Sugai19990 Sugai20004F Sugai2002% Sugano19919! 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Sun1993** Sun1998+q Sun1998 Sunada19933 Sunada19949*(Sunahara1997*1Sunahara1997$ Sund19921 Sundaralingam1992 Sundaralingam1993 Sunday19909& Sunde1997+ Sunde1998, sunde1998- Sunde1999!Sundelin1985!Sundelin1985!Sundelin1985 Sundell1992! Sunderland1993 D Sundqvist1990 Sung1992v! Sung1992v! Sung1992v" Sung19931%Sunshine1978!  Suomalainen1990  Supertifurga1991"$ Suprenant1993!  Suprenant1993 Surette1992)Surewicz1990Surewicz1991 Surewicz1991Surewicz1991 Surewicz1993! Surewicz1993 Suri1993v  Suriano1967 4 Surin1993 Surin1993B Surles19922!  Surrey1992 Surridge1990! Surridge1992! Suss1990v%Susskind19833Susskind19833#hSusskind19855" Sussman1990 Sussman1992" Sussman1993!t Sussman1993 Sutarto1992 Sutcliffe1988  Sutcliffe1991! Sutcliffe1991 Sutcliffe1991D Sutcliffe1992! Sutcliffe1992! Sutcliffe1993 Sutcliffe1993 Suter1981! Sutherland1976? Sutherland1980 land1980  Degrado1990 Degrado1990 Degrado1991 Degrado1992u Degrado1992 Degrado1992 Degrado1992 Degrado1992; Degrado1992 Degrado1992 Degrado1992 Degrado1992 Degrado1992 Degrado1993 Degrado1993 Degrado1993 Degrado1993 Degrado1993 Degrado1993 DeGrado1994 DeGrado1995*C DeGrado1997- DeGrado1999Degraeffmeeder1990Degraeffmeeder1991 Degrip1992t Degroot1993Degroote19933' Deguchi1994\Deguzman19922Dehaardhoekman1992Dehaardhoekman1993 Dehaas19911k Dehaas19929j Dehaas19929Dehaseth1990Dehaseth1992 Dehoop1993  Deibel19922 Deibel19922k Deibel19933) Deinzer1997-> Deinzer19994M Deinzer2002.Deischel19898$; Deisenhofer1992- Deisenhofer19963 Deisenhofer19997 Deisenhofer19996 Deisenhofer20006 Deisenhofer20013 Deisenhofer20026 Deisenhofer20027t Deisenhofer2002&= Deisseroth1992 5 Deitermann20038p Dejaegere2002 Dejesus1993# Dejong19911 Dejong19921 Dejong19921 Dejong19931 Dejongh1990 Dejongh1992) Dejongh1995g Dekan1993 Dekker1991 ## Dekker19911k Dekker1992j Dekker1992  Dekker1993  Dekker1993  Dekker19933 Dekroon1990 Dekroon1991 Dekroon1991 Dekroon1993 Dekroon1995) Dekroon1995) Dekroon1996) Dekroon1996 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990"T Dekruijff1990 Dekruijff1991 Dekruijff1991 Dekruijff1991#0 Dekruijff1991"U Dekruijff1991 Dekruijff1991 Dekruijff1991g Dekruijff1992 Dekruijff1992 Dekruijff1992 Dekruijff1992d Dekruijff1992 Dekruijff1992 Dekruijff1992  Dekruijff1992 Dekruijff1992 Dekruijff1992# Dekruijff1993j Dekruijff1993i Dekruijff1993 Dekruijff1993 Dekruijff1993 Dekruijff1993  Dekruijff1993  Dekruijff1994M Dekruijff1994e Dekruijff1995 Dekruijff1995 Dekruijff1995 Dekruijff1995U Dekruijff1995) Dekruijff1995)  Dekruijff1995)  Dekruijff1995 Dekruijff1995) Dekruijff1996g Dekruijff1996 Dekruijff1996N Dekruijff1996) Dekruijff1996) Dekruijff1996#+ Dekruijff1996) Dekruijff1996O Dekruijff1996Del Pozo1992 Delaat1992  Delachapelle1992 Delaet19909#Delaglio1992#Delaglio1993/Delaglio20004Delahaye1992 o Delahoz19919G Delaney19836! DeLano20004 Delarue1994# Delasierra1992 O Delasierra1993 WDelbaere19931 Delcamp1992 Deleage1993## Deleeuw1991# Delepelaire1992$L Delepierre1982 } Delepierre1991  Delepierre1995 /z Delepierre1999`| Deleppierre1991l Deleuze1992 Delfin1993 + Delfino19983 Delfino20026+ Delgado20019fDelgado-Rodrigues20059kDelgado-Rodrigues2005" Delgadopartin1993F Delgiudice1991  Delgiudice1992  Delisi19879" Delisi1990  Delisi19939&[ Delisi19939" Delisi19939/ DeLisi20000= Delisio1992 Delius19688! Deliveliotis1992 Dell1992v0X Dell'Angelica19981 Della2001 Dellabona19906 Dellwo199293 Delmas19922 Deloose1993 Z Delphin1992 Delphin1992 Delpino1992Delporte1993s Delsuc19900 Delsuc19929 Delsuc19929- Delsuc19977t Deluca19939 Deluca-Flaherty19905DeLuca-Flaherty19948DeLuca-Flaherty1994Delucaflaherty1990d Delucca1993c Delucca1993 ^DelValle19899 Delvy1993Demacedo1993Demaeyer1992I Demaio199298 DeMaio20032 Demand1998 2 Demand2000 1= Demand20014y Demand20022&1 Demarco19907 DeMarco2003,Demarest1998.ADemarest1999/NDemarest1999/Demarest2000! w Demars19909 A Demars1991 * DeMartino1998* Dembowski1998 Demchenko1993) Demchuk1997( Demel1988( Demel1988 Demel1990 Demel1991#0 Demel1991 Demel1991 Demel1992haas19929Dehaseth1990Dehaseth1992 Dehoop1993  Deibel19922 Deibel19922k Deibel19933) Deinzer1997-> Deinzer1999.Deischel19898$; Deisenhofer1992- Deisenhofer1996&= Deisseroth1992  Dejesus1993# Dejong19911 Dejong19921 Dejong19921 Dejong19931 Dejongh1990 Dejongh1992) Dejongh1995g Dekan1993 Dekker1991 ## Dekker19911k Dekker1992j Dekker1992  Dekker1993  Dekker1993  Dekker19933 Dekroon1990 Dekroon1991 Dekroon1991 Dekroon1993 Dekroon1995) Dekroon1995) Dekroon1996) Dekroon1996 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990 Dekruijff1990"T Dekruijff1990 Dekruijff1991 Dekruijff1991 Dekruijff1991#0 Dekruijff1991"U Dekruijff1991 Dekruijff1991 Dekruijff1991g Dekruijff1992 Dekruijff1992 Dekruijff1992 Dekruijff1992d Dekruijff1992 Dekruijff1992 Dekruijff1992  Dekruijff1992 Dekruijff1992 Dekruijff1992# Dekruijff1993j Dekruijff1993i Dekruijff1993 Dekruijff1993 Dekruijff1993 Dekruijff1993  Dekruijff1993  Dekruijff1994M Dekruijff1994l Dekruijff1995e Dekruijff1995 Dekruijff1995 Dekruijff1995 Dekruijff1995U Dekruijff1995) Dekruijff1995)  Dekruijff1995)  Dekruijff1995) Dekruijff1996g Dekruijff1996 Dekruijff1996N Dekruijff1996) Dekruijff1996) Dekruijff1996#+ Dekruijff1996) Dekruijff1996O Dekruijff1996Del Pozo1992 Delaat1992  Delachapelle1992 Delaet19909#Delaglio1992#Delaglio1993Delahaye1992 o Delahoz1991# Delasierra1992 O Delasierra1993 WDelbaere19931 Delcamp1992 Deleage1993## Deleeuw1991# Delepelaire1992$L Delepierre1982 } Delepierre1991  Delepierre1995 | Deleppierre1991l Deleuze1992 Delfin1993 + Delfino1998" Delgadopartin1993F Delgiudice1991  Delgiudice1992  Delisi19879" Delisi1990  Delisi19939&[ Delisi19939" Delisi19939= Delisio1992 Delius19688! Deliveliotis1992 Dell1992v Dellabona19906 Dellwo199293 Delmas19922 Deloose1993 Z Delphin1992 Delphin1992 Delpino1992Delporte1993s Delsuc19900 Delsuc19929 Delsuc19929- Delsuc19977t Deluca19939 Deluca-Flaherty1990Delucaflaherty1990d Delucca1993c Delucca1993 ^DelValle19899 Delvy1993Demacedo1993Demaeyer1992I Demaio19929&1 Demarco1990,Demarest1998.ADemarest1999 w Demars19909 A Demars1991 * DeMartino1998* Dembowski1998 Demchenko1993) Demchuk1997( Demel1988( Demel1988 Demel1990 Demel1991#0 Demel1991 Demel1991 Demel1992 6, /  0'PR Abaza, M.S.I. Atassi, M.Z. 1992Effects of Amino Acid Substitutions Outside an Antigenic Site on Protein Binding to Monoclonal Antibodies of Predetermined Specificity Obtained by Peptide Immunization - Demonstration with Region-94-100 (Antigenic Site-3) of Myoglobin"Journal of Protein Chemistry115433-444 Oct3AMINO-ACID SUBSTITUTIONS CYTOCHROME-C DETERMINANTS LACTALBUMIN LYSOZYME MONOCLONAL-ANTIBODIES MYOGLOBIN POWERFUL PREDETERMINED SPECIFICITY REGIONS RESIDUES SPERM WHALE MYOGLOBIN SYNTHETIC ANTIGENIC SITE SYNTHETIC PEPTIDESp8LFAbbadi, A. McHarfi, M. Aubry, A. Premilat, S. Boussard, G. Marraud, M. 1991AMINO-ACIDS C-ALPHA CRYSTAL LONG-RANGE INTERACTIONS MAGNETIC-RESONANCE MODEL DIPEPTIDES MOLECULAR-STRUCTURE N-GLYCOSYLATION POLYPEPTIDE-CHAINS SEQUENCE CODEpiInvolvement of Side Functions in Peptide Structures -The Asx Turn - Occurrence and Conformational Aspects.(Journal of the American Chemical Society 1137 2729-2735 27 MarjdAbbruzzetti, S. Crema, E. Masino, L. Vecli, A. Viappiani, C. Small, J.R. 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Scalettar, B.A. Hackenbrock, C.R.i 1990AGGREGATION CLUSTERS DEPENDENCE INTERACTING MEMBRANE-PROTEINS LATERAL INTERACTIONS LIGHT-SCATTERING MODEL MOLECULES MUTUAL DIFFUSION SELF-DIFFUSIONExqOn the Measurement of Particle Number and Mobility in Nonideal Solutions by Fluorescence Correlation SpectroscopyyBiophysical Journal 581o261-265` Jul15-Labeled MNT Repressor.(Journal of the American Chemical Society 113.25 9688-9690 4 Dec0 8238("Vuister, G.W. Delaglio, F. Bax, A. 1992ASSIGNMENTS C-13 CALMODULIN DEPENDENCE H-1 NMR-SPECTROSCOPY PANCREATIC TRYPSIN-INHIBITOR RESONANCE SPIN COUPLING-CONSTANTS STAPHYLOCOCCAL NUCLEASEZSAn Empirical Correlation Between 1J(CalphaHalpha) and Protein Backbone Conformation.(Journal of the American Chemical Society 114-24 9674-9675 18 Nov&!qWWW"X"AX"X"X"X#?X#X#X$#X$sX$X%XX%X&X'X(X)sX*MX*X+XXPa =a-aa"a aaYa&a anthophylluuY e ueSee aaaaafaa!a#Ta%a-a1'I171amadanakasnagisawacsukochieastoEe,se *eUe ee ewield*odarki, 's+shiharau% N ZE&6aa*anolari(zeat0 ntralblattnZhang$ooui  iegelhoffernc ppernunigae ewield*odarki+shiharau ZEa*anolari0 EntralblattZhangou  iegelhoffernc ppernunigaENza""""""""""""""<<<<<<;<;;;;;;;;;;;            ++++++HHHHHHHHHHH'R9domainshntnnOnnn n''nnnnnn[njnnn|nnn+ n:nVnznnnnnnEnnnn+nn4nnnnnnnnnnn1nnnnn <n n n!7n!n*(n"\n"en"hn#"n+n#An  荒￯$% ( !""  0 " ; ( $ " ( $ "*(  (謹  $ ( 2Gov2'2'2'2'2 '2 '2 '2 '2 '2'2'2'/'2'2'2'2'2'2'2'2'2'2'2'2!'2 '2"'2$'2%'2)'2('2''2&'2+'/'2-'2.'/'21'/'/'22'23'24'25'26'27'28'29'2:'2;'2<'2='2>'2?'2B'2@'2@'2@'2@'2@'2@'2@'. Users should consult legal counsel before using NLM-produced records to be certain that their plans are in compliance with appropriate laws. Disclaimer THE NLM DATABASES ARE INTENDED FOR INFORMATIONAL PURPOSES AND ARE NOT A SUBSTITUTE FOR MEDICAL CARE OR TREATMENT BY A QUALIFIED PROFESSIONAL. THE NLM AND THE PUBLICATION SOURCE MAKE NO REPRESENTATION ABOUT THE SUITABILITY OR ACCURACY OF THIS DATA FOR ANY PURPOSE, AND MAKE NO WARRANTIES, EITHER EXPRESS OR IMPLIED, INCLUDING THE WARRANTIES OF MERCHA109*000e00H0n0+000!M0+M0.0/#0)0#05Y0 0 0 00Q00<0H0a0 E0 0!0!0"Z0$;0%0%r00(0'002'0/06B16Y060606D'0117'78_'38'3233138282G8742G7789*101)0&0/n00 030$03216127271424,48$8,892!6#0sible surface areas of the proteins correlate linearly, providing with NMR determined self-diffusion coefficient as an additional parameter to describe quaternary structures.Article Academic Press:4Krishnan, V.V. Sukumar, M. Gierasch, L.M. Cosman, M. 2000xrDynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand 5a'077457846'0185k'842'117'937'37'372997'30Q69'999$99#9596+96.96396A96T96969696969696969696969697'97,97]979)9)9)9&5+c5+w55'404"w5442'86='73'7146'46'47s2745b'48X'81'8541'92'94'95'55'56%'56r'55'55'9575969699077 [7 7+o74'17!27677 7 9~ 9  9 9} 9} 99&5c+5w+55'404w"5442'8=6'73'714,6'4b5'41'8541'92'94'95'55'5%6'5r6'55'55'95759699077[ 7 7o+74'1 7 9~ 9 9 9} 9D SPECTROSCOPY COUPLING-CONSTANTS DISTANCE GEOMETRY MOLECULAR-DYNAMICS NMR-SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE PROTEIN-STRUCTURE PROTEIN-STRUCTURE DETERMINATION SOLUTION CONFORMATION STRUCTURE REFINEMENTtDetermination of a High-Quality Nuclear Magnetic Resonance Solution Structure of the Bovine Pancreatic Trypsin Inhibitor and Comparison with 3 Crystal StructuresL 227o3757-775 5 Octy"Journal of Molecular Biology:4Berndt, K.D. Guntert, P. Orbons, L.P.M. Wthrich, K. p x   @  12L-t h    3245$Hollecker, M. Creighton, T.E.e 1980F?Counting integral numbers of amino groups per polypeptide chain- FEBS Letters 1191A187-189  22 Sep 32480)Hollecker, M. Creighton, T.E. Gabriel, M. 1981piPreliminary circular dichroism study of the conformations of intermediates trapped during protein foldings Biochimie63 11-12835-839Nov-Dec 3246$Hollecker, M. Creighton, T.E.p 1982JCEffect on protein stability of reversing the charge on amino groupse$Biochimica et Biophysica Acta  701-3395-404M 4 Mar- 3247$Hollecker, M. Creighton, T.E.. 1983}Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom 168a2409-437M 5 Aug-"Journal of Molecular Biology 3249:4Hollenbaugh, D. Bajorath, J. Stenkamp, R. Aruffo, A. 1993ACTIVATED PLATELETS ENDOTHELIAL VONWILLEBRAND-FACTOR GMP-140 BINDS GRANULE MEMBRANE-PROTEIN LECTIN ACTIVITY LEUKOCYTE ADHESION MOLECULE-1 NEUTROPHIL ADHESION NODE HOMING RECEPTOR SCANNING MUTAGENESIS WEIBEL-PALADE BODIES^XInteraction of P-Selectin (CD62) and Its Cellular Ligand - Analysis of Critical Residues Biochemistry3212 2960-29662 30 Mar 3250Hollenbeck, P.J. 1990F?MEMBRANE PROTEIN SECRETION SEQUENCE SIGNAL RECOGNITION PARTICLEL.(Cell Motility - Dynamin Joins the Family Nature 347  6290 229 20 Sep 3251$Hollenbeck, P.J. Dentler, W.L. 1991PROTEINS.(Cell Biology - Microtubules Get the Chop Nature 350 6317378-379y 4 Apr@ 3252Hollenberg, M.D. 1991ALPHA-SUBUNIT BETA ADRENERGIC RECEPTOR EPIDERMAL GROWTH-FACTOR EXPRESSION GLUTAMATE RECEPTOR INSULIN-RECEPTOR LIGAND-BINDING MEMBRANE MOLECULAR-STRUCTURE PROTEINSXRStructure-Activity Relationships for Transmembrane Signaling - The Receptor's Turn FASEB JournalT52S178-186 FebHollien, J. Marqusee, S. 1999NHA thermodynamic comparison of mesophilic and thermphilic ribonucleases H Biochemistry38 3831-3836. JAH Hollien, J. Marqusee, S. 1999D=Structural distribution of stability in a thermophilic enzymeoProc Natl Acad Sci U S A962413674-8.10570131 JAHhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=10570131 http://www.pnas.org/cgi/content/full/96/24/13674 http://www.pnas.org/cgi/content/abstract/96/24/13674Hollien, J. Marqusee, S. 2002RComparison of the folding processes of T. thermophilus and E. coli ribonucleases H'6;B J Mol Biol 31612327-340.11851342 JAHSZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11851342 3257*$Hollosi, M. Perczel, A. Fasman, G.D. 1990ANTIFREEZE GLYCOPROTEIN CONFORMATION DERIVATIVES DIPEPTIDES GLYCOSYLATION LINKAGE MUCUS GLYCOPROTEINS PEPTIDE MODELS SIDE-CHAIN INTERACTIONS ULTRAVIOLET CIRCULAR-DICHROISMRCooperativity of Carbohydrate Moiety Orientation and Beta-Turn Stability Is Determined by Intramolecular Hydrogen Bonds in Protected Glycopeptide Models Biopolymers29 12-1 1549-1564Oct-Nov 3255@9Hollosi, M. Kollat, E. Kajtar, J. Kajtar, M. Fasman, G.D. 1990<5BONDS CRYSTAL-STRUCTURES MONOTHIATED ANALOGS PEPTIDES TNChiroptical Labeling of Folded Polypeptide Conformations - The Thioamide Probe Biopolymers30 11-1 1061-1072 3258TMHollosi, M. Urge, L. Perczel, A. Kajtar, J. Teplan, I. Otvos, L. Fasman, G.D.r 1992ALUMINUM ALZHEIMER NEUROFIBRILLARY TANGLES ALZHEIMERS NEUROFILAMENTS BETA-PLEATED SHEETS CALMODULIN CIRCULAR-DICHROISM DISEASE METAL ION TITRATIONS MICROTUBULE-ASSOCIATED PROTEIN PANCREATIC-POLYPEPTIDE PHOSPHORYLATED NF-M FRAGMENTS PORCINE NEUROFILAMENTS SUBUNIT TAU-PROTEINpjMetal Ion-Induced Conformational Changes of Phosphorylated Fragments of Human Neurofilament (NF-M) Protein 223o3673-682 5 Feby"Journal of Molecular Biology 3254Hollosi, M. Ismail, A.A. Mantsch, H.H. Penke, B. Varadi, I.G. Toth, G.K. Laczko, I. Kurucz, I. Nagy, Z. Fasman, G.D. Rajnavolgyi, E. 1992B;CLEAVAGE MEMBRANE-FUSION SEQUENCE T-CELL EPITOPES TRANSPORTo|vConformational and Functional Properties of Peptides Covering the Intersubunit Region of Influenza Virus Hemagglutinin& European Journal of Biochemistry 206 2421-425 1 Jun 3256`ZHollosi, M. Otvos, L. Urge, L. Kajtar, J. Perczel, A. Laczko, I. Vadasz, Z.S. Fasman, G.D. 1993AMINO-ACID SEQUENCE BETA-TURNS CALCIUM-BINDING CIRCULAR-DICHROISM CRYSTAL-STRUCTURE NUCLEAR MAGNETIC-RESONANCE PHOSPHOPROTEINS PHOSPHOSERINE PHOSVITIN PROTEINHBCa2+-Induced Conformational Transitions of Phosphorylated Peptides Biopolymers333497-510 Mar9 3259VPHolly, S. Majer, Z. Toth, G.K. Varadi, G. Rajnavolgyi, E. Laczko, I. Hollosi, M. 1993 SECONDARYCircular Dichroism and Fourier-Transform Infrared Spectroscopic Studies on T-Cell Epitopic Peptide Fragments of Influenza Virus HemagglutininI:3Biochemical and Biophysical Research Communications  1933S 1247-1254E 30 Jun 3262Holm, L. Sander, C. 1992hbDATABASE DESIGN PREDICTION PROTEIN FOLDING PROTEIN-STRUCTURE ROTAMERS SEQUENCE SIMULATED ANNEALINGyFast and Simple Monte-Carlo Algorithm for Side Chain Optimization in Proteins - Application to Model Building by Homology142213-223 Oct0*Proteins: Structure, Function and Genetics/Duringo7kTkEkk~kkkkkkk$kokkk Nk Zk!k"Mk# k#k)(k),k)-k+Xk+lk&kksk+sk0k0k5k6k6)k63k69k6Pk6Yk6\k6hk6jk6vk6zk6|k6}k6k6k6k6k6k6k6k6k6k6k7k7k7k7k7kAcidsi#i~ii _i i i!i!i!fi!ni!i!i"i#i#^i#i$&i$i$i%i&Oi)+i+Zi'Jii)i+oi+pi'Mi+xi+yi,i!;iNi'Si+Yi+si0i1ii4i5i6i6 i6i6i6i6i6i6i6!i6&i6>i6@i6Bi6Gi6Ji6Zi6_i6bi6bi~ Denatured i( iu i i: i i i i { i  i) i) i*{ i*z i  i A i  i  i i iC ip ir i i i i_ i'^ i_ i i i< i i'_ i i6 iZ i*| i i#@ i#] i%b i& i+ i+ i& i,= i+ i,Y i,f i,p i i, i, i i  i  i i- i- i-O i-O i#Df J.K. Hunt, H.D. Yun, T.J. Rohren, E.M. Prescott, J.L. Jobe, S.M. Allen, K.S.f 1993ALLODETERMINANTS ANTIGEN RECOGNITION SITE GENES LYMPHOCYTE-T MONOCLONAL-ANTIBODIES MUTANTS OVERLAP EXTENSION T-CELL RECOGNITIONrzs 8128RKVazquez, S.R. Kuo, D.Z. Bositis, C.M. Hardy, L.W. Lew, R.A. Humphreys, R.E.e 19926/CORE DESIGN PACKING PEPTIDES PROTEINS SEQUENCEStnResidues in the Longitudinal, Hydrophobic Strip-of-Helix Relate to Terminations and Crossings of alpha-Helic7byt7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a8a8a8a8a8a8 a8 a8a8a8a8a8a8a8a8a8a8a8a8a8a8apCYsteineTs"s s s s s s s sCsssGs_ssmss7sLshsssYs`ssss ss s ]s s s#s#s$fs$es$s%xs&{s&s)'s+qs+xs/s/s4ys6s6 s6's69s6=s6s6s6s6s7s7s7s7s7s7srts 5ressionori% squiredolding! gK g)sgionaav aaFaDalssU(ression ulated"ion o3!oryE y i  iNHARDtiiLATEd>iWionship svex5xations  e e$ eVeasei)iingmainsi!ovalr naturationlPtinol pEatsMslaced\mentsICAtion`orts5 ressionrAcylatedmi7&i7i7i \ion7 C"W C H C C C$P C7 C7 C C6  C'RCoAglycerolE4INE+ phosphatase,+t+t-rt.t0t0t6t6t7t ] transferase"R$RLR' RRRR 9R#R#VRR / RTHOSIPHOND  D)D)a)AAA A1&1161e169%agi!)i+i Siigi!)i+iirmm m:mEczewskios4INE+ phosphatase,+t+t ] transferase"R$RLR' RRRRR 9R#R#VR / RTHOSIPHOND  D)D)a)AAA A1&11e169%agi!)i+i Siigi!)i+iirmm m:mEczewskiosssLU7transferpQaaaraa a$ayapaa'aaa aaaaa a!a$Qa$Ua&a+a&a6a6a63a6Ba6Ka6aa6ha6ra6a6a6a6a6a7a74a7ia7a7a7a7a7a7a8a8 a82a8Ja8xa8ya8a8a8a8a8a8aase O  A _ A@ A       $   75 8   aa a!aQ$aU$a&a+a&a6a6a36aB6aK6aa6ah6ar6a6a6a6a6a6a7a47ai7a7a7a7aase O  A_  A@ A       $   57  654~32H10.N/0-,+*)('&%d$41:3Agback, P. Glemarec, C. Sund, C. Chattopadhyaya, J.  1992CD SPECTROSCOPY COUPLING-CONSTANTS H 1 NMR INVITRO POINT NUCLEOTIDE PROTON REGIOSPECIFIC SYNTHESIS SITE TRINUCLEOTIDES YEAST MITOCHONDRIAtSolution Structures of Nonameric and Decameric Branched-RNA Modelling the Lariat of Group-II and Nuclear Pre-Messenger-RNA Introns (Splicing) by 500 MHz NMR Spectroscopyr Tetrahedrona4831 6537-6554t 31 Jul42NHAggerbeck, L.P. Wetterau, J.R. Weisgraber, K.H. Mahley, R.W. Agard, D.A. 1988Crystallization and preliminary X-ray diffraction studies on the amino-terminal (receptor-binding) domain of human apolipoprotein E3 from serum very low density lipoproteinsa 2021P179-181 5 Jul"Journal of Molecular Biology43D=Agnati, L.F. Fuxe, K. Benfenati, F. Voneuler, G. Fredholm, B.n 1993AFFINITY DOPAMINE-D2 AGONIST BINDING INCREASES MODULATION NEUROTENSIN PROTEIN-PHOSPHORYLATION RAT STRIATAL MEMBRANES SITES SUBSTANCE-P VASOACTIVE INTESTINAL PEPTIDEvoIntramembrane Receptor Receptor Interactions -Integration of Signal Transduction Pathways in the Nervous System"Neurochemistry International223213-222 Mar2B;Ago, H. Kitagawa, Y. Fujishima, A. Matsuura, Y. Katsube, Y. 1991NGCrystal structure of basic fibroblast growth factor at 1.6 resolutionJournal of Biochemistry 110P3 360-363 SepP4445B "Journal of Molecular Biology 2341  8-13 5 Nov51voDETERMINANTS ESCHERICHIA-COLI MEMBRANE TOPOLOGY PROTEIN ASSEMBLY SEQUENCE SUBUNIT INTERACTIONS TRANSHYDROGENASE530*Ahmed, A.K. Schaffer, S.W. Wetlaufer, D.B. 1975.'Library currently receives this journalt|Nonenzymic reactivation of reduced bovine pancreatic ribonuclease by air oxidation and by glutathione oxidoreduction buffers&Journal of Biological Chemistry 25021 8477-8482e 10 Nov54*$Ahmed, M.K. Choma, C.T. Wong, P.T.T. 1992hbHigh Pressure FTIR Study of Interaction of Melittin with Dimyristoylphosphatidyl Glycerol Bilayers&Chemistry and Physics of Lipidsy63 1-2s139-148  Nov`55Ahmed, S.A. Miles, E.W. 1992B-PROTEIN BINDING ESCHERICHIA-COLI INACTIVATION MECHANISM MONOCLONAL-ANTIBODIES PYRIDOXAL 5'-PHOSPHATE SALMONELLA-TYPHIMURIUM SERINE O-SULFATE SYNTHETASEVPEvidence for 2 Conformers of the beta-Subunit of Tryptophan Synthase in Solution&Journal of Biological Chemistry 26732 23309-23317  15 Nov56.(Ahn, K.S. Szczesnaskorupa, E. Kemper, B. 1993BOVINE 17-ALPHA-HYDROXYLASE CELL-SURFACE EXPRESSION GOLGI RETENTION INTRACELLULAR-TRANSPORT LUMINAL ER PROTEINS MEMBRANE-SPANNING DOMAIN SEQUENCE SIGNAL ANCHOR TRANSMEMBRANE DOMAINxrThe Amino-Terminal 29-Amino Acids of Cytochrome-P450 2C1 Are Sufficient for Retention in the Endoplasmic Reticulum&Journal of Biological Chemistry  26825 18726-18733v 5 Sep8Ahn, T. Kim, H.i 1994PISecA of Escherichia Coli traverses lipid bilayer of phospholipid vesicles 2031326-330:3Biochemical and Biophysical Research Communicationse = </:;J9\:83456 4907:4Matsumura, M. Wozniak, J.A. Sun, D.P. Matthews, B.W. 1989XQStructural studies of mutants of T4 lysozyme that alter hydrophobic stabilizationa&Journal of Biological Chemistry 26427 16059-16066  25 Sep 4906.'Matsumura, M. Signor, G. Matthews, B.W. 1989LFSubstantial increase of protein stability by multiple disulphide bonds Nature 342L 6247291-293 16 Nov 4903"Matsumura, M. Matthews, B.W. 1989@:Control of enzyme activity by an engineered disulfide bondScience 243H 4892792-794 10 Feb 4900<5Matsumura, M. Becktel, W.J. Levitt, M. Matthews, B.W. 1989F@Stabilization of phage T4 lysozyme by engineered disulfide bonds8617 6562-6566i SepyVOProceedings of the National Academy of Sciences of the United States of America 4904"Matsumura, M. Matthews, B.W. 1991VPStabilization of functional proteins by introduction of multiple disulfide bonds 202336-356Methods in Enzymology 4905F?Matsumura, M. Saito, Y. Jackson, M.R. Song, E.S. Peterson, P.A.- 1992ANTIGENIC PEPTIDES BETA 2 MICROGLOBULIN GENE HEAVY-CHAIN HLA MOLECULES IMMUNOGENIC PEPTIDES MHC MOLECULES REGION SELF-PEPTIDES T-CELLSInvitro Peptide Binding to Soluble Empty Class-I Major Histocompatibility Complex Molecules Isolated from Transfected Drosophila-melanogaster Cellsb&Journal of Biological Chemistrys 26733 23589-23595l 25 Nov 4902>7Matsumura, M. Fremont, D.H. Peterson, P.A. Wilson, I.A. 1992rkBINDING-SITE CELLS COMPLEX CYTOTOXIC LYMPHOCYTES-T HISTOCOMPATIBILITY ANTIGEN HLA-A2 HLA-B27 IDENTIFICATIONZTEmerging Principles for the Recognition of Peptide Antigens by MHC Class-I MoleculesSciencel 257 5072927-9340 14 Aug 4908Matsuo, Y. Kanehisa, M. 1993ztAMINO-ACID SEQUENCE GENERAL METHOD PATTERN-RECOGNITION PREDICTION RELATE 2 SETS ROTATION SECONDARY STRUCTURE VECTORSF@An Approach to Systematic Detection of Protein Structural Motifs.(Computer Applications in the Biosciences92s153-159 AprhaMatsuo, H. Walters, K.J. Teruya, K. Tanaka, T. Gassner, G.T. Lippard, S.J. Kyogoku, Y. Wagner, G.n 1999~wIdentification by NMR spectroscopy of residues at contact surfaces in large, slowly exchanging macromolecular complexes .(Journal of the American Chemical Society 121 9903-9904 4909 Matsuoka, K. Nakamura, K.p 1991ENDOPLASMIC-RETICULUM GLYCOSYLATION PHYTOHEMAGGLUTININ POTATO TUBEROUS ROOTS SEEDS SEQUENCE STORAGE PROTEIN TRANSGENIC TOBACCO TRANSPORT YEAST\UPropeptide of a Precursor to a Plant Vacuolar Protein Required for Vacuolar Targetinge883s834-838 FebVOProceedings of the National Academy of Sciences of the United States of America 4910 Matsuura, J. Manning, M.C. 1993AMYLIN ANTAGONISTS CALCITONIN GENE-RELATED PEPTIDE CGRP CGRP(8-37) CIRCULAR-DICHROISM SPECTROSCOPY GROWTH-HORMONE HUMAN CGRP-(8-37) POLYPEPTIDE RELAXATION SALMON-CALCITONIN SECONDARY STRUCTURE SUBARACHNOID HEMORRHAGE TRIFLUOROETHANOLcConformation of Human Calcitonin Gene-Related Peptide (8-37) in Aqueous Solution as Determined by Circular Dichroism Spectroscopy.81Journal of Pharmaceutical and Biomedical Analysis1123 89-93 FebL~R 1846"Driessen, A.J.M. Wickner, W. 1991The protonmotive force stimulates translocation in vivo, in crude in vitro reactions, and in a purified, reconstituted reaction. Translocation activity is a function of the pH at the inner face of the membrane. Both the transmembrane pH gradient and the transmembrane elec. potential stimulate translocation. A late-stage translocation intermediate of the proOmpA preprotein completes its translocation in the absence of ATP when a protonmotive force is imposed. This completion of translocation is retarded by a factor of >3 in deuterium oxide relative to water, demonstrating that translocation involves proton-transfer reactions in rate-limiting steps. 0027-8424 886 2471-2475rlProton transfer is rate-limiting for translocation of precursor proteins by the Escherichia coli translocaseVOProceedings of the National Academy of Sciences of the United States of Americam 1843JCDriessen, A.J. Brundage, L. Hendrick, J.P. Schiebel, E. Wickner, W. 1991\VA review and discussion, with 61 refs., on (1) reconstitution of the SecY/E protein into liposomes, (2) assay of SecA translocation ATPase and translocation, (3) growth of bacteria and isolation of cytoplasmic membranes, (4) solubilization and purifn. of the SecY/E protein, and (5) functional and biochem. characterization of SecY/E protein. 0091-679X@34*#(Vectorial Transp. Proteins Membr.)147-165.Preprotein translocase of Escherichia coli: solubilization, purification, and reconstitution of the integral membrane subunits SecY /EMethods in Cell Biology 1842"Driessen, A.J.M. Wickner, W. 1991COAT PROTEIN CYTOPLASMIC MEMBRANE EXPORTED PROTEINS INNER MEMBRANE-VESICLES INVITRO MOTIVE FORCE OMPA SECA PROTEIN SECRETORY PROTEIN TRIGGER FACTORTrlProton Transfer Is Rate-Limiting for Translocation of Precursor Proteins by the Escherichia-Coli Translocase8863 2471-24753 MarVOProceedings of the National Academy of Sciences of the United States of America 1840Driessen, A.J.M. 1992rkCOLI PLASMA-MEMBRANE ESCHERICHIA-COLI INTERMEDIATE MOTIVE FORCE OMPA SECA PROTEIN SECRETION SECY/E VESICLESAhbBacterial Protein Translocation - Kinetic and Thermodynamic Role of ATP and the Protonmotive Force$Trends in Biochemical Sciences176h219-223l Jun 1839Driessen, A.J.M. 1992CYTOCHROME-C OXIDASE EXPORT INNER MEMBRANE-VESICLES MALTOSE BINDING PROTEIN MOTIVE FORCE PLASMA-MEMBRANE PRO-OMPA PROTON MOTIVE FORCE SECA SECA PROTEIN SECE SECRETION SECRETORY PROTEIN SECY TRIGGER FACTORpiPrecursor Protein Translocation by the Escherichia-Coli Translocase Is Directed by the Protonmotive ForceA EMBO Journal113n847-853 Mar 1841Driessen, A.J.M. 1993ATP BINDING ESSENTIAL COMPONENT MEMBRANE-VESICLES PHOSPHOLIPIDS PLASMA-MEMBRANE PREPROTEIN TRANSLOCASE PRESECRETORY PROTEINS PRO-OMPA PROTON MOTIVE FORCErlSecA, the Peripheral Subunit of the Escherichia-coli Precursor Protein Translocase, Is Functional as a Dimer Biochemistry3248 13190-13197  7 Dec3|Driessen, A.J.M. Dewit, J.G. Kuiper, W. Vanderwolk, J.P.W. Fekkes, P. Vanderdoes, C. Vanwely, K. Manting, E. Denblaauwen, T. 1995zsSecA, a novel ATPase that converts chemical energy into a mechanical force to drive precursor protein translocation234981-985& Biochemical Society Transactions Requiredd m m Om jm xm pm mmEmmmmmm#mymmtmmpmmmmQmjmvmmmmm m)m)m _m m!'m"2m"4m"vm#m#zm$&m%m&0m&Om),m)1m)*m+[m+\m+dm)Dm)m+m+mm0m0m0m0m0m0m0m6Am6Jm6ym6}m6m6m6m6m6m6m6m6m6m7/m7dm7gm7nm7vm7{m7m7m7m7m7m7m7m7m7m7m7m8m8-m85m8Nm8Um8nm8xm8~m8mmentSD S S SM S9 S  S  SeeeVeBvviitaneneejmanmkssonmmmmm&=Ofc&;N&MN&LN&KN&JN&IN&HN&GN&PN&ON&NN&RN*N&TN&VN&UN&WN&YN&ZN&\N&_N&`N&aN&cN&dN&eN&N&fN&N&N&N&N&N&N&N&wN&uN&tN&sN&yN&|N&{N&zN&~N&N&N&N&N&N&N)N&N&N&N&N&N&N&N&N&N&N&N&N% BIochemistry% i% i% i% i% i% i% i% i% i% i% i% i% i% i% i% i% i% i& i&  i&  i&  i& i& i&! i&" i&$ i&3 i&9 i&D i&C i&B i&A i&H i&\ i&_ i&f i& i& i& i&w i&u i& i& i& i& i& i& i& i' i)( i)( i)( i)( i)( i)( i)( i)( i)( i)( i)( i00025 u23 J42558271!92 40 0633412 6>7 j875l5001743 r415593 7239 }1 002026 4 7R8032 4|2 2 |2445 m67 8530025 u2 J42458271!92 40 0633 6 j875l50aSiGnalCciqiiiiRiSiUiTiWii i Yi i i i gi ji i i <i pi}iiiii5i6iiiXiiiiiiiti]ii iiiBiiMiOiiiiiiiiiiiiiii:4Davidson, N.O. Drewek, M.J. Gordon, J.I. Elovson, J. 1988Rat intestinal apolipoprotein B gene expression. Evidence for integrated regulation by bile salt, fatty acid, and phospholipid fluxS(!Journal of Clinical Investigationn821300-308 Julu @()J) "DLR+]FD+Fromr*S,>S+S,KS,LS,MS,NS S,S,}S,S-S- S,SS-SSS+S-*S;S,SSnSqSpSSSqS2S!=S$S*CS,S-IS,S,S-US-qS-S-S-S-S-S-S.S.S. S. S.%S.'S#(S.OS.YS.dS.pS.S.S-HS.S.S.SbFarge8iernolisiasmsd0nazzoselli8^ l lowmer&N9\N' N N!V n1y5'ington#6 ' n6' n6' nnesyl#aaa_aa a a#a-atedi i  i ion t. t  t&{ c#cysteinet#t transferaseuu*uu, u uuu s_smss6ssworthu u u u\umqqgquharrr ee e%e&zY&'!+H +O'),)+|!u}+q'P+y+++**)!w&N,'+,*&,=,E*,_*,,,,4O3,G*l)S)R'X-*n8p; H)L{}   -C-F>-ST-^-c]-e----ZMEThodsTT-TxTTgT T T T T T1TTPTTMTTTTTBTeTTTT 7T#T$,T$2T%T,FT.lT.TTT/ST0T0T1T1T3T4T+T/T6HT7T8T88T8T8T T9TNT&TTT TGTaTpTTTTTT<T)ZTTTT T T T46-95540 13 Oct 6534Ricker, R.D. Kaji, A. 1992"ALKYL PHOSPHOTRIESTERS ANTISENSE BETA-GLOBIN SYNTHESIS COMPLEX-FORMATION DNA OLIGOMER GENE-EXPRESSION MESSENGER-RNAS OLIGODEOXYRIBONUCLEOTIDE ETHYL PHOSPHOTRIESTERS OLIGONUCLEOTIDES RNA OLIGOMER SECONDARY STRUCTURE TRANSFER RIBONUCLEIC-ACID TRANSLATIONAL REGULATION VIRUS-REPLICATIONTZTStudies on Antisense Inhibition of Translation Invitro - Anomalies and Re-Evaluation FEBS Letters 3093363-3700 14 Sep WSV40a Ze e eXeTee e"e&0e e0\abb-nborg enssonw 4W!S#Ji,i-iii7rgunc!inarchuka!oboda SGOW&a+]a'Oa2'36'7 affield inn0hr1Ar4or4pr!rjo minathan n  n6 n8G'merdamy0*nkyson!p!p!!p! p!"p.p8Qton8Q'pNpNp/nad9p,pedNr/ing/r1r3r6rrupsht0vinge0e0e1e7e7e7eeattdd#b gberge+eenw).l2'l3%'l3'l4W'l4Y'l4'l4'l5c'l6~'l6'l6'l7'l7'l7'l7'l7'l8v'l8{'l8'l8'l low low993 Kenney1993k Kenney19939 Kenny1992 Kenny1992= Kent19929 Kent199+NOa+a+a,a*a a,a,a,a+a+a,$a,(a,+aaa,Ua,da+a,va+aa$xa>a,a+a- a- aa)Sa-$a-%a-&aa-aa-Ca-Fa-Ga-Ja-Ya-^a-ea-ma-ra-xa+aa-a-a-a-a-a-a-a-a-a-a.a.a.a.a.ak kkkooo Couschek F r E r& r' r) r+ r* r, r- r r r r rricesxxx 0x(xsss $0@!8j9matrixas s s !s pssscsssssssnssuss s#s"s#s#s(s.3s/s/s/ssB116j3r3~3333*M303m33\333333'3(33S333`3j333X3y3z33333 30333 3 33 3 3!3! 3!3!"3!*3!G3!R3!{3!3"3"3"3"3#D3#3#3#3$3$'3$3$3$3 p pO p p \ p  p" p) p#r p$, p$H p$ p$ p$ p% p& p) p) pC p'T p) p- p% p- p. p pnn) l)TllllQl mechanism of such remarkable binding, we have characterized complexes between the bacterial chaperone SecB and a series of ligands related to maltose-binding protein. SecB interacts at multiple sites on its polypeptide ligand. The entire SpectrOmetricM y y+Y y6 y7 y y'9 s( s( s X s+ s= s> s( s< s s9 s) s* s_ sd s s s  s s s  s! s# s) s$ s% s% s&P s( s+ s+ s+ s+ s&S s\ s  s( s-> s-C s-F s-R s-[ s- s- s- s- s- s- s.+ s.- s.> s.y s s. s. s. s. sDIMENSIONAL STRUCTURE CONFORMATIONAL TRANSITIONS FLUORESCENCE GLUTAREDOXIN PROTEINS REDUCED FORM RESIDUES RESOLUTIONzsCrystal Structure Analysis of a Mutant Escherichia-Coli Thioredoxin in Which Lysine-36 Is Replaced by Glutamic AcidI Biochemistry3219 5093-5098 18 May 5560 Nikolics, K. Seeburg, P.H. 1990 INCOMPLETEPIGonadotropin-Releasing Hormone - Gene Structure, Expression and Secretion2,Recent Progress on GnRH and Gonadal Peptides 25-33URNA%7'  ))!u+o))C'T+,-5.ji...(/F/U.i.//?031&010h0g)F01"1u222223444454x5g566F6r6w6667e7u7x7~7778{9?k)E147u7),5-j.i...(F/U/i../?/301&01h0g0F)0"1u122222344454x4g556kE)14)Sthus5Y6YwY#YYtY?YYYYY-YYYYYYYYY^YYYYY)Y&Y NY!Y!Y"yY)Y#qY#Y#Y$UY$|Y%'Y%Y&/Y&0Y)'Y),Y)1Y))Y+XY+dY+lY+{Y+Y+Y#LY,Y'SY+sY0Y#Y0Y0Y5Y5Y6Y Which l l!l!'l!fl!ol!l!l!l"l"El"Ml"ul"xl"yl"l"l)l# l#l#l#/l#zl#l#l#l#l#l#l)l$Ul$l%l%&l%'l%l%l%l&/l&Ol&_l)l)&l)(l)+l),l)-l)1l))l+Xl+[l+l+_l+al%l+dl+fl+hl+il+jll)Dl reduced <s' s4ss ssBsassss;ss)ssss$s s!'s!s#{s#s$&s&Os)-s+ys'Ss0ss6 s6s65s68s6fs6s6s7s76s7as7ms7vs7zs7}s7s7s7s7s8s8Rs8^s8is8os8s8sis 5i!Ki&ui1Ci&<i i4i6xi8$i8i6=iblenng t1tt+xt'St7at7t8t8taseFZ FY e\ e[ e e e e'1 e- ez e, e e e e eJSampling4^n9!n9"nnn5o8Uo8o%ognas80son8r+wraoui6son"nidzexovs,uel">s2onnysonz n+e n. n/' n0 n1 nn-z a/ a5 a8 a9U a9l a)$a&a+da'Sa)Fa1a'a1{'a2z'a2'a2'a2'a2'a2'a3"'a4'a4*'a4D'a4A'a4r'a4'a5I'a5|'a5'a5'a6'a6'a6'a6'a6'a6!'a6&'a61'a6E'a6v'a6'a6'a6'a6'a7'a77'a78'a79'a7o'a7p'a7'a7'a7'a7'a7'a7'a6'a8+'a8,'a83'a8'a8'a8'a ada93bonmatsu92 c chezrrkrr|r{reports123t143-187 Jun 2043 Ernst, R.R. 19923-DIMENSIONAL NMR-SPECTROSCOPY COHERENCE-TRANSFER CROSS-RELAXATION DISTANCE GEOMETRY HETERONUCLEAR 2-DIMENSIONAL SPECTROSCOPY HIGH-RESOLUTION NMR MULTIPLE QUANTUM TRANSITIONS SOLUTION CONFORMATION SPIN TOPOLOGY FILTRATION TWO-DIMENSIONAL NMRlPINuclear Magnetic Resonance Fourier Transform Spectroscopy (Nobel Lecture)e:4Angewandte Chemie - International Edition in English317805-823 Jul.0Ofc0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N1N1N1N#N#N#N1N1N1#N1N0`N/9N)/N/N"N1N1NN0N1'NN.N*NN&NN0N);N)[N0JN"NN):N)?N@N=N2N0N0N1 NSN0N1N)QN1N+ N +N! ﾻ Ϳ" ?  "( ( !"( (   ?!! (    "( (*! !$* $/EnTRezp/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o/o($뷥(  ! "淋!$!  $ (þ篯" /"$!翵$" "* %  ʫ篧 !$$￭"(!%篯 $! $$" 寭뽧%"   %!""a HEPAtOCytes t t' MMAtt"t%ppp6@p6p6phpancreasG G2d t&2ler0pners&, tacosapeptideTd TTrr'5rpppp,p7mericpeptide r  r  r r  v v8| vvalentR83Rakk kramberger bethe<te EIICIDE e$'OLA7u'decke11'r15'e1P'e1Q'e1X'e1i'e1k'e1o'e1p'e1r'e2}'e2'e2'e1j'e49'e4'e5'e5'e6'e7''e76'e7|'e7'e7'e8`'e)emses is from copyrighted publications of the respective copyright claimants. Users of the NLM databases are solely responsible for compliance with any copyright restrictions and are referred to the publication data appearing in the bibliographic citations, as well as to the copyright notices appearing in the original publicati+ofi+a+a+a+a'Sa).a+a+sa)/a)Fa'Za7?a11'a13'a14'a15'a18'a1:'a1;'a1<'a1?'a1@'a1A'a1B'a1D'a1E'a1F'a1H'a1I'a1J'a1K'a1M'a1N'a1O'a1R'a1S'a1T'a1U'a1W'a1Y'a1Z'a1['a1_'a1`'a1c'a1e'a1f'a1g'a1m'a1q'a1s'a1t'a1v'a1w'a1x'a1y'a1z'a1{'a1|'a1}'a1~'a1'a1'a1'athe connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 4 - 6... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 7 - 9... Sending message to server... Connecting to host..3( 5600 2002 Dec 64.Generating and exploiting polarity in bacteria 1942-6 Bacteria are often highly polarized, exhibiting specialized structures at or near the ends of  7155.(Shelness, G.S. Lin, L.J. Nicchitta, C.V. 1993CHARGED RESIDUES ENDOPLASMIC-RETICULUM MEMBRANE ESCHERICHIA-COLI HYDROPHOBIC DOMAIN LEADER PEPTIDASE MICROSOMAL-MEMBRANES RECOGNITION PARTICLE ROUGH MICROSOMES SECRETORY PROTEINS YEAST SEC11 PROTEINF?Membrane Topology and Biogenesis of Eukaryotic Signal Peptidasel&Journal of Biological Chemistryl 2687a 5201-5208e 5 Marm 7156F@Shen, L.M. Lee, J.I. Cheng, S.Y. Jutte, H. Kuhn, A. Dalbey, R.E. 1991~CLEAVAGE DNA GENE IDENTIFICATION INVIVO MALTOSE BINDING PROTEIN MEMBRANE MICROSOMAL SIGNAL PEPTIDASE PURIFICATION REQUIREMENTSUse of Site-Directed Mutagenesis to Define the Limits of Sequence Variation Tolerated for Processing of the M13 Procoat Protein by the Escherichia-Coli Leader Peptidase Biochemistry3051 11775-11781 24 Dec 71582+Shen, Z.M. Yang, J.T. Feng, Y.M. Wu, C.S.C.f 1992CIRCULAR-DICHROISM CONFORMATION DENATURATION FORMS HUMAN LACTOFERRIN IRON-BINDING PROTEIN CONFORMATION RESOLUTION SECONDARY STRUCTURE SEQUENCE SEQUENCE-PREDICTIVE METHOD TRANSFERRIN <5Conformational Stability of Porcine Serum Transferrin7Protein Science1 11 1477-1484 Novu 7157NGShen, R. Priebe, C. Patel, C. Rubo, L. Ting, S. Kahn, M. Sugasawara, R. 19922+ANTIBODY CATALYSIS HYDROLYSIS PEPTIDE SITESLFAn Approach for the Generation of Secondary Structure Specific AbzymesTetrahedron Lettersf3324 3417-3420 9 Jun ,&Shen, Y. Meunier, L. Hendershot, L. M. 2002Identification and Characterization of a Novel Endoplasmic Reticulum (ER) DnaJ Homologue, Which Stimulates ATPase Activity of BiP in Vitro and Is Induced by ER Stress    J Biol Chem 277O18 15947-1595611836248http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11836248 http://www.jbc.org/cgi/content/full/277/18/15947 http://www.jbc.org/cgi/content/abstract/277/18/15947,'Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105 and the Department of Molecular Sciences, University of Tennessee, Health Science Center, Memphis, Tennessee 38163.e6are6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a7a7a7a7a7a7a7a7a7 a7!a7"a7$a7%a7'a7)a7+a7.a71a73a74a75a7:a7<a7=a7@a7Aa7Ba7Ea7Fa7Ha7Ia7Ka7La7Pa7Xa7^a^7a& accretion7U"mulated+E d ! dM dR d d d7$ d7A d d i i_ i i sQ s  s s sh s s$Q s%& s&0 s0 s6 sb s= i i%& i% i6< i6 i7) i7 i7 i! ing7! o7$ o7 oT onr# r r r/ r rG r!> r$ r% r%~ r& r+ r r8L r r r rW r  r  rb r r r r rhttpin Institute'isItitsJournalKimKorea'lengthLettlistlong Magnetic methionine Methionine methionine MolecularmostncbinihnlmNMROctofofof'Ohone ParticlePeptidepeptide propensity proposedproteinProteinprotein Proteins proteinsPubMedquery Recognitionresidue Resonance RetrieverichrichSScience' Sciences' secretorysegmentsegment segments Sequence sequencesSignalsignal so qpo3nm@l9.kj 1044\UCavatorta, P. Sartor, G. Neyroz, P. Farruggia, G. Franzoni, L. Szabo, A.G. Spisni, A. 1991ALYTESIN BOMBESIN-LIKE PEPTIDES CELL LUNG-CANCER GROWTH-FACTORS LYSOLECITHIN MOLECULAR MECHANISM NEUROMEDIN-B PROTEIN SELECTIONFluorescence and CD Studies on the Conformation of the Gastrin Releasing Peptide in Solution and in the Presence of Model Membranes  Biopolymersr316653-661  May 1045NGCeccaldi, P.E. Benfenati, F. Chieregatti, E. Greengard, P. Valtorta, F. 1993ASSOCIATION CONTRACTION NERVE TERMINAL POLYMERIZATION PROTEIN-I PROTEIN-PHOSPHORYLATION SYNAPTIC VESICLE SYNAPTIC VESICLES TERMINAL-SPECIFIC PHOSPHOPROTEINnhRapid Binding of Synapsin-I to F-Actin and G-Actin -A Study Using Fluorescence Resonance Energy Transfer FEBS Letters 3293301-305 30 Aug.(Cecchini, M Rao, F Seeber, M Caflisch, A 2004TNReplica exchange molecular dynamics simulations of amyloid peptide aggregation"Journal of Chemical Physics 12121 10748-10756 KSR 1046 Cech, T.R. Uhlenback, O.C. 1994RIBOZYME HAMMERHEADG commentaryHammerhead Nailed Down Nature 372N 39-40 10474.Cejka, Z. Gouldkostka, J. Burns, D. Kessel, M. 1993(!ELECTRON-MICROSCOPY GROEL PROTEINP~wLocalization of the Binding Site of an Antibody Affecting ATPase Activity of Chaperonin cpn60 from Bordetella-pertussisI$Journal of Structural Biology 111o1 34-38Jul-Augt 1048 Celander, D.W. Cech, T.R.P 1991BINDING-SITE ENDORIBONUCLEASE ACTIVITY GROUP-I INTRONS INTERVENING SEQUENCE NUCLEAR MAGNETIC-RESONANCE PHENYLALANINE TRANSFER-RNA PROTEIN SELF-SPLICING RNA TERTIARY STRUCTURE TETRAHYMENA RIBOZYMEIF@Visualizing the Higher Order Folding of a Catalytic RNA MoleculeScience 251 4992401-407t 25 Jan"Celinski, S.A. Scholtz, J.M. 2002XQOsmolyte effects on helix formation in peptides and the stability of coiled-coilsmProtein Scienceb11 2048-20511 JAH  1049TNCellier, M.F.M. Teyssier, J. Nicolas, M. Liautard, J.P. Marti, J. Widada, J.S. 1992jcGENE HIGH-TEMPERATURE HOMOLOG INFECTION NUCLEOTIDE-SEQUENCE POLYMERASE STRESS PROTEINS TUBERCULOSISIztCloning and Characterization of the Brucella-Ovis Heat Shock Protein DnaK Functionally Expressed in Escherichia-ColiJournal of Bacteriologyc 174924 8036-8042 Dec>7Ceriotti, A. Pedrazzini, E. Desilvestris, M. Vitale, A. 1995,%Import into the endoplasmic reticulumdMethods in Cell Biologyd50295-308Methods Cell Biol. 1050HBCerneus, D.P. Ueffing, E. Posthuma, G. Strous, G.J. Vanderende, A. 19935'-NUCLEOTIDASE ANTIBODIES CANCER-CELLS COATED PITS HUMAN-FIBROBLASTS LOCALIZATION PHOSPHATIDYLINOSITOL-GLYCAN PLASMA-MEMBRANES PROTEINS SPHINGOMYELIN@9Alkaline phosphatase is anchored to the outer leaflet of the plasma membrane by a covalently attached glycosyl-phosphatidylinositol anchor. We have studied the biosynthetic. transport and endocytosis of alkaline phosphatase in the choriocarcinoma cell line BeWo, which endogenously expresses this protein. It was demonstrated that the protein was synthesized as a Triton X-100-soluble precursor. During transport to the cell surface the enzyme was converted in a mature form, which was insoluble in Triton X-100 at 0-degrees-C. Once at the cell surface 85% of alkaline phosphatase remained in the detergent-insoluble form. Under steady state conditions 15% of alkaline phosphatase was endocytosed. Most interestingly, this fraction of internalized alkaline phosphatase was completely soluble in Triton X-100 at 0-degrees-C. After depletion of membrane cholesterol by saponin, alkaline phosphatase became completely soluble in Triton X-100 at 0-degrees-C, suggesting that cholesterol plays a critical role in the formation and maintenance of Triton X-100-resistant membrane domains.nxrDetergent Insolubility of Alkaline Phosphatase During Biosynthetic Transport and Endocytosis - Role of Cholesterol&Journal of Biological ChemistryC 2685t 3150-3155t 15 FebPRotein-{!;!:$G%l F Nh-|  --.... .."* HZ'S h',...&+K++t+Y/////////////e'eBeJeMeTeUedejeeeeeeeeeee $Ыd 4475Li, Z. Hermans+Byt+_a+`a+aa+da+ea'Ja+ga+ha+ja+laa)Daaa)a+pa'Paoa)2a+ra'Qa+xa+ya+|a+}a+~a+a+a+a+a+a+aOa#La,a,a,aNa'Sasa+a+ta+Ya+sa#a0a0a0a0a0a0a0a0a0a0a0a0a0a0a0a0a0a0a/oK/pa/sa/ia/ha/da/a-a-a/Ba.a-'a/a/a/a/a%>a(aKa(a/a/a/a/a/a/a/a/a/a/a/a/a/a/a/a/a/a/aaaaaaa.=a0a0a0a0a0a0"a0-a0;a0<a0=a0>a0@a0Aa0Ba0Ca0Da0FaF0aF0a *翽" " $"$  0   竾ꮿ  "$ ("(( $ﯿ d1130&11118$10076o3406o2)?22m7082m439340.4554255.5)?6!o71Q91221Q112z2$2.3500.02a12a3!o3!n2&L7386353939824232255&5/o50!n0&L1837051P181P52+232+55374336630733775772775792992o2802o3)34 >2*22202025228s08127n15987n224&567)394C00&0!|0"0&/00{0008)055)348i330&78&A556* ￿$% ($! "*% $3$1$1$1$1$1$1$1%1%1%'1%*1%.1%C1%V1%Z1%]1%x1%1%1%1%1%1%1%1%1%1%1%1%1%1&1&1& 1&!1&,1&G1&U1&Y1&s1&y1&|1&1&1&1)61)51)+1+`1+e11'O1+g11711+q1o1+y1 1+1+1+1*1 \1j_p Arioka1993 Aripov19933 Arispe1993 8 Arispe2003Arkowitz19922Arkowitz1993+ Armand19989/ Armen2000$Armitage1990r Armitage1990'Armitage1991Armitage1993+Armitage1998 Armon19905 Armon2001U Armstrong1989 Armstrong1991 Armstrong1991 Armstrong1991 Armstrong1992  Armstrong1992 Armstrong1992  Armstrong1993 5 Armstrong1993 Armstrong1993 Armstrong1993 Armstrong1993* Armstrong19986 Arnaout20015 Arndt1991&c Arndt19930Arnesano2001 / Arnheim1989C Arnold1991  Arnold1991  Arnold1991 Arnold1991  Arnold1992  Arnold1992  Arnold1992  Arnold1992  Arnon1971 Arnone1974 G Arnone19933Y Arnosti1993- Arnoux199958 Arockiasamy2003 Aroeti1993 g Aronson1993( Aronson1996.Aronsson199736Aronsson1997Aronstam1990, Arooz1996 Arp1990 Arramond19933  Arrecis1991Arreguin1993r Arretz1991 Arrhenius1990 Arriagada19920 Arrighi2001 Arrigo1993 '] Arrington1997- Arrington1999/ Arrington20005 Arrington20000 Arrington2001 Arriza19922  Arrondo1992c Arrondo1992 Arrondo1993 Arrondo1993 Arrowsmith1991 Z Arrowsmith1992 &U Arrowsmith1993'W Arrowsmith1994 % Arrowsmith1994  Arrowsmith1996 1 Arrowsmith1998Q1 Arrowsmith2000Q1 Arrowsmith20020Arseniev19919Arseniev1992fArseniev19922Arseniev19922Arseniev19939Artavanistsakonas1993  Arterburn1993 Artur1993 RArtymiuk1985Artymiuk1986Artymiuk1993.sArtymiuk1997@hArtyukov19931 Aruffo19939+ Arulanandam1993*X Arvai1997 Arvan1991 Arvan1992 Arvan1993 Arvidsson1993 Arvinte1993 Arvinte1993 Arzt19911 Asada19910> Asada19990A Asada1999 Asahi1993 Asai19900 Asai19929 Asai1993v) Asai19969I Asakawa1993$ Asakura1992$ Asakura1992) Asakura1993 Asakura1993 Asakura19936{ Asakura1993! 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Atkins19999Atkinson1990 Atkinson1991Atkinson1991 Atkinson1992Atkinson19939Atkinson19939 fAtkinson19939Atkinson1993!fAtkinson19931 hAtkinton19949  Atreya1991 4[ Atreya200229_ Attar20059X Attar2005 Attie1992 Attila199396 Attwell1992  Attwood1993  Atwal1992*b Atwell1997  Atwood1991  Aubert19921- Aubert1999 Aubin1993 Aubrey1991  Aubrey19939 Aubry1991E Aubry1992 Aubry1992"? Aubry1993 Aubry1993 Aubry1993 Auchincloss1992 Audebrand1993 Aue1976. Auer19959* Auer1998v Auerbach19922 Auerbach1993Auerbach19939TAuerbach2004l& auf der Mauer1993 Auger1991'/ Auger1993'. Auger1993  August19939 Augusteyn1993 Augustine1993. Augustine19991; Augustine20013 Augustine2001 Aulak1988'; Aulak1989 Auld19933> Auluck2002< Aumailley1991 1 Aumailley1992  Aumailley1992t Aumailley1993 Aune1967v Aune1969v Aune1969v- Aune19739 Aurora1993m Aurora1994* Aurora1997 * Aurora1998* Aurora1998 # Ausio1993/< Austen19877X Austen1990 - Austen19909 Austen1996 Austin199392b Austin19999 Austoni1993 Autiero1993 SAutiliogambetti1992 Avbelj1990 -  Avbelj19908 Avbelj1993* Avbelj1998 5 Avbelj20034 Avdeeva20024 Avdeeva20027 Avdeeva2002 Aviel1992 Avila1990 Avila1991 Avila1991 Avila1991 Avila1992 Avila1992 d Avila19923 Avila1993a Avila1993 Avila1993 Avila1993" Aviles1982kq Aviles19929  Aviles1992 , Aviles19959*F Aviles199797 Aviles19989/ Aviles20000+ Avils19989 Avital1991   Avni1991v!Avoustin1992" Avril1993 Avron1990 Avron1990# Avron1991- Axe1999z Axelsen1991$ Axelsen1991 Q Axelsen1992) Axelsen1998& Axmann1994 q AYa1993- Ayed19991 Ayed200004- Ayed2002m*B Ayemerich1997% Ayer1991v. Ayers1999/ Ayers19991 Ayers19992 Ayers20022+ Aygun2001-} Ayling1996"H Aymami19929& Azem1994v6" Azem19959 Azerad19933# Azhar1993( Azize1991' Azuaga1992 , Azuaga199595q Azuaga2003varsson1994 f B.1988i! B:avik19858 Baart1992) Baas1993v$ Baase1988 Baase1989 Baase1989e Baase1990j Baase1991h Baase1991g Baase1991f Baase1991 Baase1991&9 Baase1991 Baase19923 Baase1992 Baase1992 Baase1992 Baase1992  Baase1992" Baase1992b Baase1992&@ Baase1992% Baase1992 Baase19931993e1976* Auer1998v Auerbach19922 Auerbach1993Auerbach1993& auf der Mauer1993 Auger1991'/ Auger1993'. Auger1993 Augusteyn1993 Augustine1993 Aulak1988 Aumailley1991 1 Aumailley1992t Aumailley1993 Aune1967v Aune1969v Aune1969v Aurora1993m Aurora1994# Ausio1993X Austen1990  Austen1996 Austin19939 Austoni1993 Autiero1993 Avila1991 Avila19923 Avila1993a Avila1993" Aviles1982kq Aviles19929z Axelsen1991 Q Axelsen1992% Ayer1991v"H Aymami19929& Azem1994v Azerad19933( Azize1991' Azuaga1992  Baart1992) Baas1993v$ Baase1988 Baase1989 Baase1989e Baase1990j Baase1991h Baase1991g Baase1991f Baase1991 Baase1991 Baase19923 Baase1992 Baase1992 Baase1992 Baase1992 Baase1992  Baase1992" Baase1992b Baase1992 Baase19934PRObesii Li >iiiHiii:i;iliiii>i%$i+ri'Ti7ii6i"yi+i+_i+ii4i7Hi7Ii7oi7i7i8=i8i(ingLlllll l Ql l0lQlll>llllll(lyl;llYlUll l+6l%l,ll,l,l@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@@@@@ @@@@@22@@@@@@@@@@@@@@@@@2@@@@@2@@@@@@@@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@99@@@@@@@@@@@9@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@@@@@@2@@@@@@@@@@@@@@@@@@@@@2@@@@@@@@@@@@@@9229@@@@@2@@@@@@@9@@@@@@@9999@@@@@@@@?;Surface*S;SSSMSiS%SWSVSSSSS S S S S+S ;S DS eS S S ;S MS S S S S 1S S SSSS$S)SXSaS SS#S7S9SSSS)S7S}SSSSSSwSiSSSkSkSkStSLightlymm!m#m$&m'Qm0m6m6m6m7Lm7m8gm ~m81e7:engsby6w*wkowskioan)n2y'm3'm5'm6?'m6'm6'm7,'m8P'mmianynimsss.ski6}pe8[t8[s tb(boomwwkwjw7ten4A'venia5'iiterwwiji(i i ti li Ni i_i]i`iiii''iiii4iiicii$i$i&i%4i%=i+i+i i i@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@@@@9@@@@2@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@@@9@@@@@@@@@@@@@@@@@@@@9@@@@ @@@@@@@@@@@@@@@@@@p *AssemblyiiiiignedRments  s  o&Jstixociated i i i+ iion( t X v  v5 vet-;ymmetricktkk6k!uk &kkekk"4k)rk+k'W'k)kinsonP'omic,P!a aa8a(aase!jt T T*~T1T+ainablewoodLugs %s sBsTsQsPsgsss uststeni tOimmunityr  Regulatory&Vena ianhhhh-hh%hhhHhHHODO z@@$HRupleysjsrsperth3rrecht&WTURE _s ss`cacccUcmcccc5c8cUcWcYc!a!a" a" a"a"#a"~a"}a2 RElaxationi aW a a. a a a a a a a% aG a a a a8 ad a a6 a ad a M a u a  a  a!{ a! a" a" a" a" a# a# a# a# a$ a% a&D a&[ a  ap ap aq a, a/ a{ a!: a! a av a#' a#$ a#% a] a at a a2 a& a) aO a% aNCambierlllau o o!ourCridgeD P- P- P P P) P) P) P) P) e) e) e) e)' e)5 e+o e+p e+w e+ e+ e e1F' e1' e3&' e4'' e42' e47' e4X' e4^' e4i' e4' e4' e4' e5H' e5X' e5W' e5\' e5[' e5' e5' e5' e5' e5' e5' e6' e6O' e6n' e6' e6' e6' e6' e6' e6' e7' e7' e7!' e7*' e7;' e7<' e7H' e7x' e7~' e7' e7' e7' e7' e7' e7' e8?' e8H' e8[' e8f' e8n' e8' e8' e e*7RERjoS."l."ized4SPIN'USRA$t" inioteroont5t#t.kt0ttti ino P~ P  P P} P PPP_P P P P/ Structure* s0 s.4 s07 s08 s- s0j sJ s s s0r s0 s0 s0 s0y s0 s s0 s0 s# s# s1 s1 s0 s1' s s. s* s1 s  s/} s0 s1A s1[ s1s s1 s1 s1 s1 s1 s1 s1 s1 s1 s1 s1 s1 s. s1 s/ s2 s2% s2& s s/ s25 s2> s2? s2E s2N s2N s2N s()(('F4&T%!"..+? v 745 Bowie, J.U. Eisenberg, D.@ 19933-DIMENSIONAL STRUCTURE AMINO ACID SEQUENCES ASSOCIATIVE MEMORY HAMILTONIANS FOLDS GLOBULAR-PROTEINS IDENTIFICATION LOCAL INTERACTIONS MEAN FORCE TEMPLATES TERTIARY STRUCTURE RECOGNITION,%Inverted Protein Structure Prediction,%Current Opinion in Structural Biology 33r437-444 Jun 752JCBowler, B.E. May, K. Zaragoza, T. York, P. Dong, A.C. Caughey, W.S. 1993DIRECTED MUTAGENESIS ELECTROSTATIC INTERACTIONS INFRARED-SPECTRA LAMBDA-REPRESSOR PROTEIN STABILITY SACCHAROMYCES-CEREVISIAE SOLVENT DENATURATION STAPHYLOCOCCAL NUCLEASE THERMODYNAMIC STABILITIES YEAST ISO-1-CYTOCHROMES-C Destabilizing Effects of Replacing a Surface Lysine of Cytochrome-c with Aromatic Amino Acids -Implications for the Denatured StateO Biochemistry321y183-190 12 Jan 753>7Bowman, S. Ackerman, S.H. Griffiths, D.E. Tzagoloff, A. 1991ATPASE COMPLEX ESCHERICHIA-COLI MEMBRANE SYSTEM PRECURSOR PROTEIN IMPORT SACCHAROMYCES-CEREVISIAE SEQUENCE-ANALYSIS STRUCTURAL GENE SUBUNIT TRANSLOCATIONSnhCharacterization of ATP12, a Yeast Nuclear Gene Required for the Assembly of the Mitochondrial F1-ATPase&Journal of Biological ChemistryL 26612 7517-7523i 25 Apr:3Bowser, D. Minamikawa, T. Nagley, P. Williams, D.A.@ 1998b\Role of Mitochondria in Calcium Regulation of Spontaneously Contracting Cardiac Muscle CellsBiophysical Journal 75October 2004-2014 JAHh.'Bowyer, P.J. Swanson, A.G. Morris, G.A. 1999iRandomized acquisition for the suppression of systematic F1 artifacts in two-dimensional NMR spectroscopy : @; $Journal of Magnetic Resonance 140513-515d SJE 757("Boyd, J. Dobson, C.M. Redfield, C. 1985lfIdentification of glycine spin systems in 1H NMR spectra of proteins using multiple quantum coherences FEBS Letters 1861 35-40 1 Jul 756("Boyd, J. Dobson, C.M. Redfield, C. 1985HAAssignment of resonances in the 1H NMR spectrum of human lysozyme& European Journal of Biochemistry 1532H383-396 2 Dec- 758.(Boyd, L.F. Kozlowski, S. Margulies, D.H. 1992ASSOCIATION EQUILIBRIUM H-2LD HLA MOLECULES IMMUNOGENIC PEPTIDES INFLUENZA PEPTIDES KINETICS LIGAND LIGAND PROGRAM LYMPHOCYTE-T MEMBRANES MURINE CYTOMEGALOVIRUS RECEPTOR SURFACE T-CELL RECOGNITIONSolution Binding of an Antigenic Peptide to a Major Histocompatibility Complex Class-I Molecule and the Role of beta2-MicroglobulinG896H 2242-2246H 15 MarVOProceedings of the National Academy of Sciences of the United States of Americas 754(!Boyd, D. Traxler, B. Beckwith, J.r 1993`YBINDING-PROTEIN COMPONENTS DEPENDENT TRANSPORT-SYSTEMS ESCHERICHIA-COLI PERMEASE SEQUENCEnhAnalysis of the Topology of a Membrane Protein by Using a Minimum Number of Alkaline Phosphatase FusionsJournal of Bacteriology 1752553-556 JanBoyden, M.N. Asher, S.A. 2001f`UV Raman studies of peptide conformation demonstrate that betanova does not cooperatively unfold Biochemistry4045 13723-13727Nov. 135PROTEIN SECONDARY STRUCTURE, AQUEOUS-SOLUTION, FOLDING FUNNELS, SHEET PROTEIN, LASER SOURCE, HAIRPIN, GENOMICS, DYNAMICS, DESIGN, NMR\VWe used UV resonance Raman spectroscopy (UVRR) excited within the peptide bond pi --> pi* electronic transitions and within the aromatic amino acid pi --> pi* electronic transitions to examine the temperature dependence of the solution conformation of betanova, a 20-residue P-sheet polypeptide [Kortemme, T., Ramirez-Alvarado, M., and Serrano, L. (1998) Science 281, 253-256]. The 206.5 nm excited UVRR enhances the amide vibrations and demonstrates that betanova has a predominantly beta -sheet structure between 5 and 82 degreesC. 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Yayon, A. 1993VPBASIC-FGF CLONING DNA EXPRESSION FAMILY FGF RECEPTOR FORMS GENES MEMBER PROTEINSMultiple Structural Elements Determine Ligand Binding of Fibroblast Growth Factor Receptors - Evidence That Both Ig Domain-2 and Domain-3 Define Receptor SpecificityT&Journal of Biological Chemistry  268l11 7899-7903 15 Apr3091I1u1 1 1 1G1W11*1&|1/714m151'11110L0306^0X0 0%1 S 2s2)3 3 3 4 5 6 7 7 8 9mers4111)16171133,333 3 3 3 3 t3 333333333 K3!3,373333z3 [3'3 3 33393=3333333(3#3$|3%3%3+l3+3, 3}3)3M3132M32V33V34`35363637383 3333C3`3_3^3]3q3}3}3_3^3]3q3}3.ZC./A.A*A.A.A/AA/vA,A/A.A/A/AxAtA0A0A0!A0A0A0A0A0A)QAlA13A1@A1A1A1A2uA2A2A3*A3+A3A3A3A4A4A44A4TA4]A4AA5zA5A5A5A5A5A6;A6BA6hA6A7OA7VA7\A7qA7xA7A7A7A8A8 A8 A8$A8cA8tA8yA8A8A9A9GA=AA!A' A A A A!V A$ A/I A8 A' AD A A A A A) A!V A4 AAA Aa+3A3A3A3A4A4A=AA!A' A A A AV! A$ AI/ A' AD A A A A A) AV! 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Vershon, A. Bouvier, S. Sauer, R.T. Susskind, M.M. 1983:3Ch #T"####"#|#, N. Ledbetter, D. Kootwijk, E. Vaessen, M.J.CATION SEQU `< øVaessen, M.J ` < øon of Membra `panning Amino Acid Residues Be Responsible for the Recognition of Signal Peptides by Signal Peptide PeptidasesBioscience Reports106A537-5460 Dec `@7( 7186(!Shin, J. Lee, S. Strominger, J.L.  1993>8CD4 CELL RECEPTOR COMPLEX ER MEMBR 8077F?Vanderleij, I. Franse, M.M. Elgersma, Y. Distel, B. Tabak, H.F.s 19933-KETOACYL-COA THIOLASE BIOGENESIS FIREFLY LUCIFERASE IDENTIFICATION MUTANTS PEROXISOME PROTEIN IMPORT SNAP HELIX TARGETING SIGNAL TERMINUS TRANSCRIPTION YEASTiPAS10 is a Tetratricopeptide-Repeat Protein That is Essential for the Import of Most Matrix Proteins into Peroxisomes of Saccharomyces-cerevisiae9024 11782-11786 15 DecVOProceedings of the National Academy of Sciences of the United States of Americai 8079.'Vandermeer, B.W. Cheng, K.H. 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Ploegh, H.L. 1992CDC4 GENE COMPLEX G-PROTEIN BETA-SUBUNIT GENE-PRODUCT GLUCOSE REPRESSION PROTEIN BETA-SUBUNIT PROTEIN FAMILY PRP4 SACCHAROMYCES-CEREVISIAE SHOWS HOMOLOGY TPR-GENE FAMILY TUP1 WD-40 REPEAT YEASTThe WD-40 Repeat FEBS Letters 3072131-134 28 Jul7 Campbell19979)Campbell1998+ACampbell1998+Campbell19989,Campbell1998.Campbell19999/Campbell2000!3-Campbell2002w7HCampbell20027Campbell2002* Campbell-Burk1991* Campbell-Burk1992 Campbellburk1992 Campbellburk1992! Campbellburk1992` Campese1993 Campetella1993 " Campion19904 Campo2002! Campos199446 Canady1993 / Canals200027p Canaves2002` Candela1992q Candia19799# Candy1992+R Cane1998 Canel1991- Canet19990 Canet20023, Canet20023I Canet20025q Canet20036 Canet2003$Canfield1991Canfield1992& Cann1987 Cann199296  Canne1998. Canne1999 Cannon19933 Canters1991" Canters1991# Canters19920 Cantini2001'/ Cantley1993'. 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Carpenter1993 Carpenter1993 ' Carpenter1993 ( Carpenter1995, Carpenter1997+ Carpenter1998/ Carpenter2000'0 Carpentier1993  Carr19909'2 Carr1991v'1 Carr1991v' Carr19911'3 Carr1992v$ Carr19929'5 Carr1993v'4 Carr1993v'6 Carr19945 Carr2002, Carra1994'7 Carrara1992 Carrascosa1988  Carrascosa1992 h Carrascosa1993  Carrascosa1993 '9Carraway1993'8Carraway1993 Carrell1988@ Carrell1988 Carrell1988 Carrell1988 Carrell1988Y Carrell1988': Carrell1988 Carrell1988A Carrell1989 Carrell1989 Carrell1989G Carrell1989 ~ Carrell1989C Carrell1989B Carrell1989 Carrell1989'; Carrell1989f Carrell1989W Carrell1990$ Carrell1990  Carrell1990&4 Carrell1990 Carrell1990 Carrell1991 Carrell1991 Carrell1991 Carrell1991D Carrell1991'< Carrell1991% Carrell1991# Carrell1991 Carrell1992 Carrell1992G Carrell1992 Carrell1992, Carrell1997, Carrell19982Carrello1999D Carreno1992'= Carreno1993'> Carrera1993'? Carrey1993  Carri1993zCarrillo1990UCarrillo1992Carrillo19939  Carrington1990 K Carrington1993 7 Carrio20007 Carrio20017 Carrio20027 Carrio2003-Carrion-Vazquez1999.Carrion-Vazquez1999V Carroll1990 Carroll1992 Carroll1993$ Carron19929? Carron19933K Carrupt1992W Carson1991 F Carson19922#S Carson199330Carswell2001$ Carter19849% Carter1984X Carter1984  Carter198595959 Carter19859 Caputo1997 7 Cara1995v Caradonna1993Carafoli19922#Carafoli1992#Carafoli19938 Caraty1990  Carazo198889Carbajal1990 Carbon19933 Carbone1993,a Carbonell1998 o Carbonero1991s Cardamone1992t Cardamone1993ZCardemil1993 Carden1993 Cardillo1992; Careaga1992: Careaga1992& Carelli1993n Carey1992! Carey1992z Carey1993` Carey1993%a Carey1993,} Carfi1998%Cargnoni1992DCariappa19955Carlacci1991Carlacci1991<Carlacci1993 4 Carlemalm1993 Carlier1991 Carlier1993= Carlino1992> Carlone1993&Carlotti1993% Carlson1991 Carlson1993', Carlson1993 Carlsson19922Carlsson19933'+Carlsson1995> Carlstedtduke1993 Carmichael1993  Carney19888S Caron1991 Caron1992 Caron1992? Carpenter1987  Carpenter1992'- Carpenter1992  Carpenter1992 Carpenter1993'/ Carpenter1993'. Carpenter1993 Carpenter1993 ' Carpenter1993 ( Carpenter1995, Carpenter1997+ Carpenter1998'0 Carpentier1993  Carr19909'2 Carr1991v'1 Carr1991v' Carr19911'3 Carr1992v$ Carr19929'5 Carr1993v'4 Carr1993v'6 Carr1994'7 Carrara1992 Carrascosa1988  Carrascosa1992 h Carrascosa1993  Carrascosa1993 '9Carraway1993'8Carraway1993 Carrell1988@ Carrell1988 Carrell1988 Carrell1988 Carrell1988Y Carrell1988': Carrell1988 Carrell1988A Carrell1989 Carrell1989 Carrell1989G Carrell1989 ~ Carrell1989C Carrell1989B Carrell1989 Carrell1989'; Carrell1989f Carrell1989W Carrell1990$ Carrell1990  Carrell1990&4 Carrell1990 Carrell1990 Carrell1991 Carrell1991 Carrell1991 Carrell1991D Carrell1991'< Carrell1991% Carrell1991# Carrell1991 Carrell1992 Carrell1992G Carrell1992 Carrell1992, Carrell1997, Carrell1998 Carreno1992'= Carreno1993'> Carrera1993'? Carrey1993  Carri1993zCarrillo1990UCarrillo1992Carrillo19939  Carrington1990 K Carrington1993 V Carroll1990 Carroll1992 Carroll1993$ Carron19929? Carron19933K Carrupt1992W Carson1991 F Carson19922#S Carson19933$ Carter19849% Carter1984X Carter1984  Carter198599859$H&/)  836:3Brower, R.C. Vasmatzis, G. Silverman, M. Delisi, C. 1993"GLOBULAR PROTEIN MONTE-CARLO^WExhaustive Conformational Search and Simulated Annealing for Models of Lattice Peptides Biopolymers0333I329-334 MarBrown, J. E. Klee, W. A. 1971JDHelix-coil transition of the isolated amino terminus of ribonuclease Biochemistry10470-476 Brown, S. Fournier, M.J. 1984BThe 4.5S RNA gene of Escherichia coli is essential for cell growth  &  J. Mol. Biol.d 178533-550  853*$Brown, W.B. Larrabee, W.A. Kim, P.S. 19866/Analysis of a leprosy-specific antibody epitopeCLeprosy Review 57 Suppl 2157-162 DecBrown, Stanley 1987b\Mutations in the gene for EF-G reduce the requirement for 4.5S RNA in the growth of E. coli. Cell49825-833 840<6Brown, D.L. Taylor, S.J. De Peters, E.J. Baldwin, R.L. 1989|vInfluence of sometribove, USAN (recombinant methionyl bovine somatotropin) on the body composition of lactating cattleJournal of Nutrition 1194 633-638m Apr 837*#Brown, B.M. Bowie, J.U. Sauer, R.T. 1990<6Arc repressor is tetrameric when bound to operator DNA Biochemistry2951 11189-11195f 25 Dec 852 Brown, S. 1991^WCLONING VEHICLES CONSTRUCTION PROMOTER SEQUENCE SIGNAL RECOGNITION PARTICLE TRANSLATIONiXQGenes for 7S RNAs Can Replace the Gene for 4.5S RNA in Growth of Escherichia-Coli8Journal of Bacteriology 173P5 1835-1837 MarO 846leBrown, L.R. Nygard, N.R. Graham, M.B. Bono, C. Braciale, V.L. Gorka, J. Schwartz, B.D. Braciale, T.J. 1991A VIRUSES BINDING-SITE CELL RECOGNITION CHEMICALLY SYNTHESIZED PEPTIDES FINE SPECIFICITY IA IMMUNOGENIC PEPTIDES STRUCTURAL CHARACTERISTICS SYNTHETIC PEPTIDES VIRUS HEMAGGLUTININRecognition of the Influenza Hemagglutinin by Class-II MHC-Restricted Lymphocytes-T and Antibodies .1. Site Definition and Implications for Antigen Presentation and Lymphocyte-T Recognition3Journal of Immunologyt 14718 2677-2684 15 Oct 843Brown, J.D. Beggs, J.D. 1992BINDING HEAT-SHOCK HELA-CELLS PRE MESSENGER RNA PRE-MESSENGER-RNA SPLICING PROTEIN SACCHAROMYCES-CEREVISIAE SMALL NUCLEAR RIBONUCLEOPROTEIN SNRNP-SNRNP INTERACTIONS SNRNPS SPLICEOSOMAL RNA SPLICEOSOME U4 YEAST YEAST SPLICEOSOMESB;Roles of PRP8 Protein in the Assembly of Splicing Complexesp EMBO Journal1110 3721-3729o Oct 851 Brown, R.E. 1992D=Spontaneous Lipid Transfer Between Organized Lipid Assemblies0$Biochimica et Biophysica ActaO 1113 3-4G375-389O 11 Dec 8502,Brown, N.G. Fowles, C. Sharma, R. Akhtar, M. 1992ACTIVATION ADRENERGIC-RECEPTOR KINASE BOVINE RHODOPSIN CATTLE PHOTORECEPTOR MEMBRANES CYCLIC-GMP GTP-BINDING PROTEIN METARHODOPSIN PHOSPHODIESTERASE ROD OUTER SEGMENTS SYNTHETIC PEPTIDEStmMechanistic Studies on Rhodopsin Kinase - Light-Dependent Phosphorylation of C-Terminal Peptides of Rhodopsino& European Journal of Biochemistry 208e3659-667 15 Sep 849JDBrown, M.S. Goldstein, J.L. Paris, K.J. Burnier, J.P. Marsters, J.C. 1992ALPHA-SUBUNIT CLONING COVALENT MODIFICATION DPR1 EXPRESSION GERANYLGERANYLTRANSFERASE P21(RAS) PROTEINS PEPTIDE BINDING PROTEIN PRENYLATION RAS PROTEINSTetrapeptide Inhibitors of Protein Farnesyltransferase - Amino-Terminal Substitution in Phenylalanine-Containing Tetrapeptides Restores Farnesylation8917 8313-8316 1 SepMVOProceedings of the National Academy of Sciences of the United States of America. 847 1992 3-DIMENSIONAL PROTEIN STRUCTURE 3-DIMENSIONAL STRUCTURE ACETYLCHOLINE RECEPTOR ALPHA-NEUROTOXIN BINDING BUNGAROTOXIN ENERGY REFINEMENT NAJA MOSSAMBICA MOSSAMBICA NMR DISTANCE GEOMETRY REFINED CRYSTAL-STRUCTURE SECONDARY STRUCTURE SNAKE NEUROTOXINS TORPEDO-CALIFORNICAT|Nuclear Magnetic Resonance Solution Structure of the alpha-Neurotoxin from the Black Mamba (Dendroaspis-Polylepis-Polylepis) 2274 1118-1135I 20 Oct"Journal of Molecular BiologyBrown, L.R. Wthrich, K.("Brown, K.L. Wood, S. Buttner, M.J. 1992Isolation and characterization of the major vegetative RNA polymerase of Streptomyces coelicolor A3(2); renaturation of a sigma subunit using GroELMolecular Microbiology69 1133-1139 845 0950-382X 848D>Brown, M.B. Edmonds, T.E. Miller, J.N. Riley, D.P. Seare, N.J. 1993ALBUMIN ALPHA-1-ACID GLYCOPROTEIN BINDING BIOMEDICAL APPLICATIONS DRUGS HUMAN-SERUM NILE RED PROBE SOLID-STATE SPECTROFLUORIMETRY SURFACES VERY NEAR INFRARED FLUORESCENCEZTNovel Instrumentation and Biomedical Applications of Very Near Infrared FluorescenceAnalystn 1184a407-410i Apr 844b\Brown, J.H. Jardetzky, T.S. Gorga, J.C. Stern, L.J. Urban, R.G. Strominger, J.L. Wiley, D.C. 1993$X-RAY CRYSTALLOGRAPHY HLA-DR10ZTThree-Dimensional Structure of the Human Class II Histocompatibility Antigen HLA-DR1 Nature 364 33-39P 842,&Brown, E.D. Yada, R.Y. Marangoni, A.G. 19931,2-0-DILAURYL-RAC-GLYCERO-3-GLUTARIC ACID-RESORUFIN ESTER CONFORMATION DIFFERENCE KINETICS LIPASE MICROEMULSIONS MYELIN BASIC-PROTEIN OIL PROTEIN-MEMBRANE INTERFACE INTERACTION REVERSE MICELLE SOLUBILIZATIONThe Dependence of the Lipolytic Activity of Rhizopus-Arrhizus Lipase on Surfactant Concentration in Aerosol-OT/Isooctane Reverse Micelles and Its Relationship to Enzyme Structure$Biochimica et Biophysica Actai 11611t 66-72 15 Jan 841Brown, E.D. Wood, J.M. 1993ACTIVATION BINDING DEHYDROGENASE ENZYME ESCHERICHIA-COLI FLAVOPROTEINS OXIDATION-REDUCTION PURIFICATION PYRUVATE OXIDASE SALMONELLA-TYPHIMURIUMiConformational Change and Membrane Association of the putA Protein Are Coincident with Reduction of Its FAD Cofactor by Proline &Journal of Biological Chemistryi 268r12 8972-8979 25 Apr 839F@Brown, C.R. Martin, R.L. Hansen, W.J. Beckmann, R.P. Welch, W.J. 1993CHAIN BINDING-PROTEIN EXPRESSION HEAT-SHOCK PROTEIN HSP70 MAMMALIAN-CELLS NUCLEAR RECOVERY RNA THERMOTOLERANT CELL TRANSLOCATIONThe Constitutive and Stress Inducible Forms of hsp-70 Exhibit Functional Similarities and Interact with One Another in an ATP-Dependent FashioniJournal of Cell Biologyh 120 5 1101-1112 MarN/W/a/aiaaa-a-a/a0 a)a0a0a/apaa0'a05a0Qa0La)aJa0ta0a0a0a0a0a0a0a0a0a0a0|a0a0a0a0a0a0a0a0a0a0a0a#a1a0aa)0aa.a);a)Qaza0a1$a0a0a13a1Ca1Ka1KaK1aK1a1989W Shortle1989 Shortle1989$E Shortle1990X Shortle1990 Shortle1990  Shortle1990 Shortle1991 Shortle1991 Shortle1992Z Shortle1992Y Shortle1992 Shortle1992  Shortle1992  Shortle1992_ Shortle1993_ Shortle1993^ Shortle1993] Shortle1993 Shortle1993f Shortle1994*} Shortle1995-0 Shortle1995*| Shortle1996` Shortle1996, Shortle1996'^']folding(r)r/br(r+rr/r/r/r/r/r/r/r/r/r/r/r/r/r/r/r/r/r/r/rrr/r/r/r+r$r"r#'r#&r#$r#%r0r.Hr/r0r0r0r0 r/r)r0r0r0r0r0r0r0r0r0r0r0r0r0r0r0r0rx(Itzhaki+u+u-u+u&u&u+u&u*wu,u+u.Luu)u/u+u(u1u3u4iu+ueuB4MBiYchi2.r4PACVVVVVJJ) z \z a aTaaasava)aBaFaa%sa+yaa/a%aa -aa#a&OAA7uA7A7A&&A3pnkov5xoovyy*Va2skaIyi#uushinasshchukkienbaumi%B1pR1q11r11s1t1u1v1w1x1y1z1{1|1}1~1111111111111111111111111111111111111111111111111111111 1992AFFINITY BINDING-SITE ALPHA-SUBUNIT DELTA-SUBUNIT ELECTRIC ORGAN GEL-ELECTROPHORESIS H-3 CHLORPROMAZINE MEMBRANE-PROTEIN NONCOMPETITIVE BLOCKERS SODIUM DODECYL-SULFATE TRANSMEMBRANE TOPOLOGYd]Mapping the Lipid-Exposed Regions in the Torpedo-Californica Nicotinic Acetylcholine Receptor2 Biochemistry3115 3738-3750  21 Apr Blasie, C. A. Berg, J. M.  19972+Electrostatic Interactions across a -sheet Biochemistry36 6218-6222 JAH eDaofp#~p3HminsjpiniphpgppupEr#BIr#Br0c0r5'pling8tomycin8 r8 r8 r8 r8 r9 r9 r9 r9  r9 r9 r3Arabie+gankblbonyyyrnrmrorprqr"d#'d#&d#$d#%drdel*n%gsgemontK0 K K"Mo"o&Zo&ooo6nbrough2bton godarigoo szonV7l'tmouthveau7wtwishssus g gg{g!g)g, g2g6guguptawsvsh!hxh810 0 >0 0 0 0 0 Y0 0 0 0 00F0z000A000;00b0000000G0Q0b0g0 0b0j0p0)Y00z0000000%00I0000(0j0i000000000                   ///////////////...........bbbbb p 0+ ~  [ ~ &Lopez-Hernandez, E. Serrano, L. 1996xrStructure of the transition state for folding of the 129 aa protein CheY resembles that of a smaller pro<    4187Kutyshenko, V.P. 1991LFDENATURED STATE LYSOZYME PROTON RELAXATION RIBONUCLEASE SPIN DIFFUSIONXRApplication of the NMR Method to Measuring the Molecular Mass of Globular Proteins BiofizikaA365t754-757CSep-Oct4-Kuwajima, K. Nitta, K. Yoneyama, M. Sugai, S. 1976NHThree-state denaturation of alpha-lactalbumin by guanidine hydrochloride"Journal of Molecular Biology 1062 359-373P 15 Sep 4198 JAHP 4189 Kuwajima, K. 1977^XA folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism 1142N241-258 5 Aug"Journal of Molecular Biology 4205Kuwajima, K. Sugai, S. 1978tmEquilibrium and kinetics of the thermal unfolding of alpha-lactalbumin. The relation to its folding mechanism Biophysical Chemistryg833247-254 Jult 4199& Kuwajima, K. Ogawa, Y. Sugai, S. 1979jcApplication of the pH-jump method to the titration of tyrosine residues in bovine alpha-lactalbumini Biochemistry185878-882 6 Mar 4197& Kuwajima, K. Nitta, K. Sugai, S. 1980zsIntramolecular perturbation of tryptophans induced by the protonation of ionizable groups in goat alpha-lactalbuminr$Biochimica et Biophysica Actam 623N2389-401 26 Jun 4200& Kuwajima, K. Ogawa, Y. Sugai, S. 1981b[Role of the interaction between ionizable groups in the folding of bovine alpha-lactalbuminbJournal of Biochemistry 893759-770 Mara*$Kuwajima, K. Kim, P.S. Baldwin, R.L. 1983uStrategy for trapping intermediates in the folding of ribonuclease and for using 1H-NMR to determine their structuressQ  R Biopolymers5221f 59-67a Jan  4196 JAHU 4193 Kuwajima, K. Baldwin, R.L. 1983rkNature and locations of the most slowly exchanging peptide NH protons in residues 1 to 19 of ribonuclease S 1691281-297 5 Sep"Journal of Molecular Biology 4192 Kuwajima, K. Baldwin, R.L. 1983\VExchange behavior of the H-bonded amide protons in the 3 to 13 helix of ribonuclease S 16901299-323 5 Sep*"Journal of Molecular Biology6/Kuwajima, K. Hiraoka, Y. Ikeguchi, M. Sugai, S. 1985VOComparison of the transient folding intermediates of lysozyme and a-lactalbumin Biochemistry24874-881>7Kuwajima, K. Yamaya, H. Miwa, S. Sugai, S. Nagamura, T.r 1987tnRapid formation of secondary structure framework in protein folding studied by stopped-flow circular dichroism FEBS Letters 221s12115-118 31 Aug 4206 JAH8 4190 Kuwajima, K. 1989vpThe Molten Globule State as a Clue for Understanding the Folding and Cooperativity of Globular-Protein Structure62t 87-1030*Proteins: Structure, Function and Genetics 4195BI,I,IlI(ItII[IwI->I-NI-I I-I-I.$I.+I.-I.2I.3I.CI.mI.yI.zI.I.I.I.I.I.I.I.I.I.I.I.II.IIII3NCbi3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d4d4d4d4d4d4d4d4-d4,d4+d4*d4(d4'd4&d42d43d48d47d46d45d44d4;d4Hd4Gd4Fd4Ed4Dd4Cd4?d4Ad4@d4>d4<d41d4Id4IdI4d4:d4:d4:dO4dO4dO4dAmino*N6N@NDNFNNNNN(NN/N3NONVNWNNNNN*NQN\NNNNNNN/NVNUN]NNN*N N $N .N N N N!N!*N!N!N!N"?N"BN"FN"LN)N"oN"N#N#FN#EN#uN#N#N#N#Nxt68007c1u2w23 C1111111x9-.4y5,q5,6z6{6}7|869011M22#22Y2e2h2)2$S0- 0600012~33,4567992'821 71 111^1.0.V0.f0/%01 002^06311122345,6666788|93,gOfc,kN,lNN,pN,qN,rN,tN+N+N&N)N,uN,vN,xN,yNN,|N,~N,N,N,N,N,}N,N,N*N*wN,N,NNNN,N,N,NbN,N,N,N,N,NNWNVNN,N,N,N+N,N,N,N,N.N9N9N9N9N9N9N9N9N9NNSc)c)c+c+cc*c)c+c,$c,%c,&c,'c,(c,)c,*c,,c,-c,.c,0c+c,7c,4cc,:c,;c,<c*c,1ccc]c#Ic#Lc*c*c*c,Ac* c&c\c c,Icc cc,Rc+Pc,Zc,_c,`c)c,cc,dc&c&c&c&c&c&c&c&c&cleux19929| Baleux19939 Baleux19966 Bali19939 Bali19933 a Ball19900 Ball1990v Ball19919 Ball1993n Ball19939) Ball19988Ballarin1992% Ballery1990 Ballery1993)(Ballesta1997 Ballesteros1992 Ballesteros1992) Ballew1996 , Ballew1996+ Ballew19988 Ballinger1991 a Bally1990y Balmain1993 Balschmidt1992  Baltensperger1993*^ Balt8)}~  3610:4Johnson, V.G. Nicholls, P.J. Habig, W.H. Youle, R.J. 1993FRAGMENT-B GENE LOW PH MEMBRANE TRANSLOCATION NUCLEOTIDE-SEQUENCE OVERLAP EXTENSION PLANAR LIPID BILAYERS PROLYL ISOMERASE PROTEIN TRANSLOCATION VERO CELLSODiphtheria toxin (DT) can translocate across endosomal membranes in response to low pH. Buried hydrophobic domains localized in the 37-kDa toxin B chain become exposed in response to acidic conditions and are thought to participate in the membrane translocation process. The crystal structure of DT has revealed a structurally distinct translocation domain composed of nine alpha-helices with their interconnecting loops (Choe, S., Bennett, M., Fujii, G., Curmi, P., Kantardjieff, K., Collier, R., and Eisenberg, D. (1992) Nature 357, 216-222). Two of these alpha-helices, TH8 and TH9, are unusually apolar and constitute the central core of the translocation domain. It has been proposed that these domains and the highly charged interconnecting loop undergo a conformation change under acidic conditions producing a dagger-like structure capable of inserting into the membrane thus initiating the translocation process. Proline 345 occupies a strategic location at the end of the TH8 alpha-helix. Proline residues have the ability to undergo a cis-trans isomerization reaction and because of this have been proposed to play a role in the conformational change that is a prerequisite for toxin translocation. The role of the proline at position 345 in membrane translocation was investigated. Pro was mutagenized to Glu and to Gly using a two-step recombinant polymerase chain reaction procedure, and the mutant proteins were expressed in vitro. Glu, an alpha-helix former, and Gly, an alpha-helix breaker, were selected for mutagenesis to distinguish between a structural role for Pro as an alpha-helix breaker and alternative roles, perhaps involving cistrans isomerization-related conformational changes. Replacing Pro at position 345 with Glu or Gly resulted in a 99% reduction in toxicity to Vero cells. The enzymatic and binding activity of the toxin were not altered by the mutations. Instead, the reduction in toxicity is due to decreased translocation ability, suggesting that the Pro at position 345 plays a specific role in toxin membrane translocation.p@9The Role of Proline-345 in Diphtheria Toxin Translocationn&Journal of Biological Chemistrya 268t5 3514-3519 15 Feb 36094-Johnson, M.S. Overington, J.P. Blundell, T.L.C 19931.8-A RESOLUTION 3-DIMENSIONAL STRUCTURE ALIGNMENT AMINO ACID SEQUENCES AMINO-ACID SUBSTITUTIONS BINDING-PROTEIN CRYSTAL-STRUCTURE DISTANTLY RELATED PROTEINS ESCHERICHIA-COLI PATTERN-RECOGNITION PROTEIN FOLDS REFINED STRUCTURE SEARCHING SECONDARY STRUCTURE`ZAlignment and Searching for Common Protein Folds Using a Data Bank of Structural Templates 2313735-752 5 Jun"Journal of Molecular Biology Johnson, L.N. Barford, D.  1993NHThe Effects of Phosphorylation on the Structure and Function of Proteins<6Annual Review of Biophysics and Biomolecular Structure TNAnnual Reviews Inc, 4139 El Camino Way, PO Box 10139, Palo Alto, CA 94303-089722199-232 3608f`ALLOSTERIC MECHANISM BACILLUS-SUBTILIS BACTERIAL PHOSPHOTRANSFERASE SYSTEM CATALYTIC SUBUNIT CYCLIC AMP, DEPENDENT PROTEIN KINASE ESCHERICHIA-COLI GLYCOGEN PHOSPHORYLASE GRAM-POSITIVE BACTERIA HISTIDINE-CONTAINING PROTEIN ISOCITRATE DEHYDROGENASE NUCLEAR MAGNETIC-RESONANCE PHOSPHATE RECOGNITION SITES PROTEIN-PHOSPHORYLATION SIGNAL-TRANSDUCING PROTEIN*$Johnson, R.S. Krylov, D. Walsh, K.A. 1995:4Protein mobility within electrosprayed peptide ions."Journal of Mass Spectrometry??380-387 SJE NHJohnson, A.E. Liao, S. Lin, J. Hamman, B. Do, H. Cowie, A. Andrews, D.W. 1995The environment of nascent secretory and membrane proteins at the endoplasmic reticulum membrane during translocation and integration60 71-82>73rd Cold Spring Harbor Symposia on Quantitative Biologyy !\!L!~!l!!D!!$!!$!! E ZYMOGENVf_Crystal Structure of Cobra-Venom Phospholipase-A2 in a Complex with a Transition-State AnaloguePScience 250o 4987 1560-1563 14 DecFuller1 4 7h 8440*#White, T.B. Berget, P.B. Nall, B.T. 1987Changes in conformation and slow refolding kinetics in mutant iso-2-cytochrome c with replacement of a conserved proline residue,%Taniuchi, H. Anfinsen, C.B. Sodja, A. 1967vpThe amino acid sequence of an extracellular nuclease of Staphylococcus aureus. III. Complete amino acid sequence&Journal of Biological Chemistry@ 24220 4752-4758d 25 Oct 7745 7742"Taniuchi, H. Anfinsen, C.B.h 1968f`Steps in the formation of active derivatives of staphylococcal nuclease during trypsin digestion&Journal of Biological Chemistryc 243b18 4778-4786 25 Sep 7749.(Taniuchi, H. Mor:avek, L. Anfinsen, C.B. 1969Ligand-induced resistance of staphylococcal nuclease and nuclease-T to proteolysis by subtilisin, alpha-chymotrypsin, and thermolysinu&Journal of Biological Chemistry 244 17 4600-4606  10 Sep 7743"Taniuchi, H. Anfinsen, C.B.h 1969VOAn experimental approach to the study of the folding of staphylococcal nucleasen&Journal of Biological Chemistry 244r14 3864-3875 25 Jul 7744"Taniuchi, H. Anfinsen, C.B.h 1971Simultaneous formation of two alternative enzymology active structures by complementation of two overlapping fragments of staphylococcal nucleaseo&Journal of Biological Chemistry 24687 2291-2301 10 Apr 7748.(Taniuchi, H. Davies, D.R. Anfinsen, C.B. 1972|A comparison of the x-ray diffraction patterns of crystals of reconstituted nuclease-T and of native staphylococcal nuclease&Journal of Biological Chemistry  24710 3362-3364 25 MayB;Taniyama, Y. Yamamoto, Y. Nakao, M. Kikuchi, M. Ikehura, M. 1988`Role of disulphide bonds in folding and secretion of human lysozyme in Saccharomyces cerevisiae. G _  152.962-967-:3Biochemical and Biophysical Research Communicationsc60Taniyama, Y. Yamamoto, Y. Kuroki, R. Kikuchi, M. 1990Evidence for difference in the roles of two cysteine residues involved in disulphide bond formation in the folding of human lysozyme. 265 7570-7575P&Journal of Biological Chemistry 7752(!Taniyama, Y. Seko, C. Kikuchi, M.g 1990tnBOMBARDMENT MASS-SPECTROMETRY DISULFIDE BONDS EXPRESSION GENE PROTEIN SACCHAROMYCES-CEREVISIAE SEQUENCE TISSUEd^Secretion in Yeast of Mutant Human Lysozymes with and Without Glutathione Bound to Cysteine-95&Journal of Biological Chemistry 26528 16767-16771 5 Oct6 7750<6Taniyama, Y. Kuroki, R. Omura, F. Seko, C. Kikuchi, M. 1991voBINDING EXPRESSION GENE PROTEIN SACCHAROMYCES-CEREVISIAE SECRETION STABILITY STABILIZATION SUBTILISIN BPN YEASTb\Evidence for Intramolecular Disulfide Bond Shuffling in the Folding of Mutant Human Lysozyme&Journal of Biological Chemistryl 266.10 6456-6461 5 Apre 775181Taniyama, Y. Ogasahara, K. Yutani, K. Kikuchi, M.n 1992D=ALPHA-LACTALBUMIN DISULFIDE BONDS INTERMEDIATE RESIDUES STATEYf_Folding Mechanism of Mutant Human Lysozyme C77/95A with Increased Secretion Efficiency in Yeasta&Journal of Biological Chemistryd 267p7r 4619-4624a 5 Marl 77562,Tanji, Y. Gennity, J. Pollitt, S. Inouye, M. 1991rkESCHERICHIA-COLI EXPORT LIPOPROTEIN OUTER-MEMBRANE PROTEIN PHOE POSITIVE CHARGE RECOGNITION REGION SEQUENCEXREffect of OmpA Signal Peptide Mutations on OmpA Secretion, Synthesis, and AssemblyJournal of Bacteriology7 1736m 1997-2005m Mar2J2a2a2a1ja1Va2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a3a3a3a3 a3 a3 a3a3a3a3a3a3a3a3#a3$a3%a3&a3'a3-a3.a3:a3@a3Na3ca3ca3563603:03903803703@03;03<03=03>03?0303P03O03N03K03L03M03S03R03Q020303f03e03d03c03b03a03`03_03^03]03\03[03Z03Y03X03W03V03U03l03r03v03m03q03w03s03k03t03u03o03n03x03j03p03z03{03|03}03~03~03~0z FLUOREscencei t( t: tB tF tG tH tI t t t t t tj t  t t t t t  t t  tI ti tt t t t t t t t t t1 t t t tq t t t t t t t t? t t t t  t  t  t  t! t" t" t# t" t#; t#B t# t3'R3(3)3*3+3,3-3.3/303132333435363:3938373@3;3<3=3>3?33P3O3N3K3L3M3S3R3Q233f3e3d3c3b3a3`3_3^3]3\3[3Z3Y3X3W3V3U3l3r3v3m3q3w3w3i+++++++)))))))))))--------$$$$$$$$00000000""""""""////&&&&&&&&&&,,,,,"X"X"X"X"X"X"X"X"X"X"X"X"X-#1''111111""""""""11111111111111111///////////////&&&:::::::ysZ F,](X7*rUo+;&(%rc-pZM+-Q 9'Y&!( ($X !m%"3'U H|;^w!K(.$U&\,%m%mpqk< ni1k,aV*,(t*yq2ykk ~b%=;wy J#--s|*=6( u+- %REB jQ,6-q}-4/;D,f(nyc(3wy,$ (6}x-'r,lvDB %m #.n,&cv~Middaugh1993Middaugh1993Middaugh199392 Middaugh1995w Middleton1993X Midgley1992_ Midgley1993 Miehe1993 Miercke1993 Mierke19900 Mierke1990 X Mierke19901W Mierke19901 Mierke1991  Mierke1991  Mierke1992  Mierke1992  Mierke19929 Mierke19929 Mierke19933 Mierke1993  Mierke19939 Miernyk1992 Miernyk1992,B Miesenbock1998s Mieskes1993 Miettinen1992Miggiano1992-Miginiac-Maslow1997 Migliaccio1991  Migliaccio1992  Migliorini1990 8 Mignot2003 Mihaly19933 Mihara19909 Mihara19909 Mihara19919 Mihara19922b Mihara19922' Mihara19939% Mihara19939 Mihara19939 V Mihara19939 Mihara19969 Miick1991! Miick1992  Miick1992 u Miick1993" Miick1993 Miick1993 Mikami19922 Miki1987i Miki19871 Miki1992 Miki19929 Miki1992" Miki1993 Miki19931 Miki19933 Miki19944" Miki1994 Miki1996/ Miki20000 Mikkelsen1993% Miklos1992  Miko19929 " Mikoshiba1991"7 Mikoshiba1991s Mikou1990# Mikulik1993 QMilanesi1993/D Milanovich1994$ Milburn1991 Milburn19921  Mildvan1972 Mildvan1986 Mildvan1987 Mildvan1989* Mildvan1990$E Mildvan19905 Mildvan1992+ Mildvan1993.0 Mildvan1999 Miles1986% Miles1987 W Miles1987 Miles1987& Miles1988 X Miles1988! Miles1988m Miles1990' Miles19914 Miles1992' Miles1992( Miles19937)Milewski2002) Milgram1993@ Milgrom1992. Milhollen1999* Milik1992, Milik1993) Milius1994 . Miljanich1985 Miljanich1993. Milkereit19956 Milkereit19953 Mill20020, Milla199523 Milla1995, Milla19982 Millan19959 Millar19900 Millar1991  Millar19922 U Millar19929 Millar1993r/ Millar1993  Millar1993 36 Millar2001r2 Millar200222 Millard2002 Miller1980r0S Miller1982W Miller1986 0 Miller1987 $ Miller1988 x Miller19889 Miller19898$C Miller1989 Miller199001 Miller1990 4 Miller19909 Miller19919# Miller1991 4 Miller1991 3 Miller1991 2 Miller1991 Miller19929 Miller19922 Miller19929 i Miller199228 Miller1992 7 Miller1992 6 Miller1992 5 Miller1992n Miller1992y Miller1992  Miller199228 Miller19922 Miller19933 Miller19939 Miller19939 Miller19939? Miller1993? Miller19939X Miller19939 k Miller19939> Miller1993 = Miller1993 < Miller1993 ; Miller1993 : Miller1993 9 Miller1993 + Miller19939h Miller19949@ Miller1994 A Miller1995 +z Miller19977,d Miller1997-$ Miller1997h-j Miller199795 Miller19979+  Miller1998 ,I Miller1998.) Miller19999.< Miller1999t.< Miller1999t/ Miller19991/, Miller199910+ Miller1999i1x Miller199996 Miller199910 Miller20000 Miller20011 Miller2001177 Miller2001078 Miller200103 Miller200203 Miller2002t8[ Miller200339^ Miller20033,A Miller-Auer1998. Millet19999/ Millet2000"1 Millet2002<8 Millet200228 Millet20025> Millet20035 Millet2003 7 Millet20033- Millett1999. Millett19991 Millett20025 Millett2002 Millhauser1991 "* Millhauser1991 ! Millhauser1992   Millhauser1992 B Millhauser1992 u Millhauser1993 " Millhauser1993   Millhauser1993 & Millhauser1997 CMilligan1989DMilligan1991Milligan1991$Milligan19916>Milligan19959'K Millman19970 Millman2001E Mills1979* Mills1991+ Mills1992F Mills1992E Milne19933  Mierke19939 Miernyk1992 Miernyk1992,B Miesenbock1998s Mieskes1993 Miettinen1992Miggiano1992-Miginiac-Maslow1997 Migliaccio1991  Migliaccio1992  Migliorini1990  Mihaly19933 Mihara19909 Mihara19909 Mihara19919 Mihara19922b Mihara19922' Mihara19939% Mihara19939 Mihara19939 V Mihara19939 Mihara19969 Miick1991! Miick1992  Miick1992 u Miick1993" Miick1993 Miick1993 Mikami19922 Miki1987i Miki19871 Miki1992 Miki19929 Miki1992" Miki1993 Miki19931 Miki19933 Miki19944" Miki1994 Miki1996/ Miki200002A Miki20000 Mikkelsen1993% Miklos1992  Miko19929 " Mikoshiba1991"7 Mikoshiba1991s Mikou1990# Mikulik1993 QMilanesi1993/D Milanovich1994$ Milburn1991 Milburn19921  Mildvan1972 Mildvan1986 Mildvan1987 Mildvan1989* Mildvan1990$E Mildvan19905 Mildvan1992+ Mildvan1993.0 Mildvan1999 Miles1986% Miles1987 W Miles1987 Miles1987& Miles1988 X Miles1988! Miles1988m Miles1990' Miles19914 Miles1992' Miles1992( Miles1993) Milgram1993@ Milgrom1992. Milhollen1999* Milik1992, Milik1993) Milius1994 . Miljanich1985 Miljanich1993. Milkereit1995, Milla199523 Milla1995, Milla1998 Millar19900 Millar1991  Millar19922 U Millar19929 Millar1993r/ Millar1993  Millar1993 2 Millar20022 Miller1980r0S Miller1982W Miller1986 0 Miller1987 $ Miller1988 x Miller19889 Miller19898$C Miller1989 Miller199001 Miller1990 Miller19919# Miller1991 4 Miller1991 3 Miller1991 2 Miller1991 Miller19929 Miller19922 Miller19929 i Miller199228 Miller1992 7 Miller1992 6 Miller1992 5 Miller1992n Miller1992y Miller1992  Miller199228 Miller19922 Miller19933 Miller19939 Miller19939 Miller19939? Miller1993? Miller19939X Miller19939 k Miller19939> Miller1993 = Miller1993 < Miller1993 ; Miller1993 : Miller1993 9 Miller1993 + Miller19939h Miller19949@ Miller1994 A Miller1995 +z Miller19977,d Miller1997-$ Miller1997h-j Miller19979+  Miller1998 ,I Miller1998.) Miller19999.< Miller1999t.< Miller1999t/ Miller19991/, Miller199910+ Miller1999i1x Miller199990 Miller20000 Miller20011 Miller20011,A Miller-Auer1998. Millet19999/ Millet2000"1 Millet2002<- Millett1999. Millett19991 Millett2002 Millhauser1991 "* Millhauser1991 ! Millhauser1992   Millhauser1992 B Millhauser1992 u Millhauser1993 " Millhauser1993   Millhauser1993 & Millhauser1997 CMilligan1989DMilligan1991Milligan1991$Milligan1991'K Millman19970 Millman2001E Mills1979* Mills1991+ Mills1992F Mills1992E Milne1993lne1993  52200.)M 2+Fekkes, P. Denblaauwen, T. Driessen, A.J.M.o 1995jcDiffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB Biochemistry3431 10078-100850(!SecB is a chaperone dedicated to protein translocation in Escherichia coli. SecB binds to a subset of precursor proteins, and targets them in a translocation-competent state to the SecA subunit of the translocase. The nature and kinetics of the interaction of SecB with polypeptides were studied by spectroscopic techniques using the reduced form of bovine pancreatic trypsin inhibitor (BPTI) as a model substrate. Binding of SecB to BPTI resulted in an increase in the fluorescence of the surface-exposed tryptophan residue 36 of SecB. SecB reversibly binds BPTI in stoichiometric amounts. Labeling of BPTI with the fluorophore acrylodan allowed the analysis of the binding reaction at nanomolar concentrations. High-affinity binding (KD of 5.4 nM) of labeled BPTI to SecB resulted in a blue shift of the acrylodan emission maximum and an increase in the fluorescence quantum yield, suggesting that BPTI binds in an apolar environment. Stopped-flow acquisition of rate constants of complex formation between SecB and BPTI yielded a second-order binding rate constant of 5 x 10(9) M-1 s-1, and a dissociation rate constant of 48 s-1. These data demonstrate that in vitro, the association of SecB with polypeptide substrates is limited by the rate of collision. In vivo, SecB binding is selective, and predominantly occurs with nascent polypeptides. Since these chains are not expected to fold into stable structures, SecB association may be governed by "more or less" specific interactions and be limited by the rate of chain elongation rather than the rate of folding.R2+Fekkes, P. van der Does, C. Driessen, A. J. 1997The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation EMBO Journal1620 6105-6113 SSGf_Fekkes, P. de Wit, J. G. van der Wolk, J. P. Kimsey, H. H. Kumamoto, C. A. Driessen, A. J.p 1998Preprotein transfer to the Escherichia coli translocase requires the co-operative binding of SecB and the signal sequence to SecA. Mol Microbiol295 1179-1190JDFekkes, P. de Wit, J. G. Boorsma, A. Friesen, R. H. Driessen, A. J. 19994.Zinc stabilizes the SecB binding site of SecA. Biochemistry3816 5111-5116 SSG*$Fekkes, Peter Driessen, Arnold J.M.>7Protein Targeting to the Bacterial Cytoplasmic Membrane 1999 Microbiol. Mol. Biol. Rev. Microbiol. Mol. Biol. Rev.161-173n631r81http://mmbr.asm.org/cgi/content/abstract/63/1/161  March 1, 1999eProteins that perform their activity within the cytoplasmic membrane or outside this cell boundary must be targeted to the translocation site prior to their insertion and/or translocation. In bacteria, several targeting routes are known; the SecB- and the signal recognition particle-dependent pathways are the best characterized. Recently, evidence for the existence of a third major route, the twin-Arg pathway, was gathered. Proteins that use either one of these three different pathways possess special features that enable their specific interaction with the components of the targeting routes. Such targeting information is often contained in an N-terminal extension, the signal sequence, but can also be found within the mature domain of the targeted protein. Once the nascent chain starts to emerge from the ribosome, competition for the protein between different targeting factors begins. After recognition and binding, the targeting factor delivers the protein to the translocation sites at the cytoplasmic membrane. Only by means of a specific interaction between the targeting component and its receptor is the cargo released for further processing and translocation. This mechanism ensures the high-fidelity targeting of premembrane and membrane proteins to the translocation site. 2140nhFelder, S. Zhou, M. Hu, P. Urena, J. Ullrich, A. Chaudhuri, M. White, M. Shoelson, S.E. Schlessinger, J. 1993CYTOPLASMIC SIGNALING PROTEINS EGF-RECEPTOR GROWTH-FACTOR RECEPTORS PDGF RECEPTOR PHOSPHATIDYLINOSITOL 3'-KINASE PHOSPHOLIPASE-C REGULATES INTERACTIONS SRC HOMOLOGY REGION-2 SUBSTRATE TRANSDUCTION~SH2 Domains Exhibit High-Affinity Binding to Tyrosine-Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange$Molecular and Cellular Biology133 1449-1455 Margard, P.O. Kihlgren, A. Svensson, M. Carlsson, U. 1993ALPHA-LACTALBUMIN CIRCULAR-DICHROISM FOLDED APOMYOGLOBIN INTERMEDIATE GUANIDINE-HYDROCHLORIDE DENATURATION MOLTEN-GLOBULE STATE PROTEIN STABILITY UREACharacterization of Folding Intermediates of Human Carbonic Anhydrase .2. Probing Substructure by Chemical Labeling of SH Groups Introduced by Site-Directed Mutagenesis Biochemistry321y224-231 12 Jan Martin, J. 1991 Nature 352  36-4262222M2]2y222222'2*2N2*H2[2f2&2222<2H2X2a2~222282L2r2x2222/2B2d2)2&2u2222222222 u2 z2 2 2 2 2!2!2!'2!02!02RRRRRRRR_@\Peptidessssisxssss*ssssssssssssss&s.s^srsuare$aXaaaaaaaaaalaaaaa#a$aoaaaaaaa4ada)aaa Na [a _a a a!Da!na!a!a!a!a"Ma"ya"a"a)a# a#a#/a#0a)a#^a#za#{a#a#a#a)a)a)a)a)a)aV Pincus1992  Pincus19933 Pincus1993  Pincus1993  Pind1990e Pinder1992  Pineda1993  Pineiro1990 Pineiro1990 Pines1990 Pines1991T Pines1992 Ping1993 Pingoud1990* Pinhasi-Kimhi1989 MPinheiro1993*Pinheiro1997( Pinilla1997 Pinkasfeld1993 Pinkaskramarski1992 Pinker1993  Pinker1993 \ Pinker1993  Pinker1994 Pinkne,ofc47nCndngn)n)n&nnnRi n Nn Yn Zn [n \n _n n R  n n n!n!n!'n!D!fn!o!nn!n)n!!n!!n!n"n"2n"4"Cn"En"Mn"u"vn"xn"wn"yn"R"i""n)n# n#R#R#R#RYNEIN SENSITIVE SITES URCHIN SPERM FLAGELLA1rlATP-Insensitive Interaction of the Amino-Terminal Region of the beta-Heavy Chain of Dynein with Microtubules Biochemistry3213 3456-34603 6 Apr 5219ZSMoczko, M. Dietmeier, K. Sollner, T. Segui, B. Steger, H.F. Neupert, W. Pfanner, N. 1992CARRIER IMPORT RECEPTOR MITOCHONDRIAL OUTER MEMBRANE MOM19 OUTER-MEMBRANE PROTEIN PRECURSOR PROTEINS PROTEIN TRANSLOCATION VIABILITY YEAST MITOCHONDRIAiVPIdentificaHSp90QQ!aQ#Q$Q-|Q/%Q1Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q3Q4'Q4CQ5Q83Q8|QQ QksPssPssss sss!Os!s-|ss*swsSI83A8|A8A1B8.55BP1ISs QQSQ*Q*QQQ!aQ#Q$Q-|Q/%Q1Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q2Q3Q4'Q4CQ5Q8%Q8&QQ QksPssPssss sss!Os!s-|ss*swsSI8%A8&A8A1B8%55BP1ISs QQSQ*QHolmDNAjooooo&oooo;oFoGoooGoVooooooooNoYoooooo,o`ogoxoooooooooo<oMoLogoo Io jo o o(o*o o!o*So!Zo!Zo!Zo!Zo!Zo!Zo.DtRypsinpttttttZtitttbtt<tt~ttttttt,t+t/tVttttttt!t$t2tottt0t`tt#tttttttt>tttttt!t!:t!t!t!t"t"  LYSOSOMAL MEMBRANE-GLYCOPROTEINS OLIGOSACCHARIDES PROTEIN SEQUENCELocalization of the Signal for Rapid Internalization of the Bovine Cation-Independent Mannose 6-Phosphate/Insulin-Like Growth Factor-II Receptor to Amino Acids 24-29 of the Cytoplasmic TailL&Journal of Biological ChemistryS 2669 5682-5688u 25 MarF@Cann, J.R. London, R.E. Unkefer, C.J. Vavrek, R.J. Stewart, J.M. 1987<5International Journal of Peptide and Protein Research29486-496dj Sanders1992 Sanders1992 Sanders19937q Sanders2001 Sanderson1990 Sanderson1991 wSandgren19922"Sandgren199335cSandgren20032Sandhoff1990 Sandkvist1990  Sandkvist19929a Sandler2005,( Sandman1998& Sandor19933 Sandoval19912Sandoval2000e Sandri1992r Sands1993 Sands1993  Sandulache1988 Sandvig1991P Sandvig1992) Sanejouand1998  Sanford1991 Sanford1993 Sang199332 Sang19979 Sanger1952  Sanger1959R Sanger19969Sanghera19923Sangster20027\ Sangwa1998 Sani1990v#U Sani19966s Sankar19911Sankaram1990+_Sankaram1994Sankararamakrishnan1991Sankararamakrishnan1992Sankararamakrishnan1993 Sano19927s Sano20000 Sansom1991  Sansom1991  Sansom1992  Sansom1993  Sansom1993 { Sanson19922z Sanson19922| Sanson19933 Sanson19966 Sant1992v) Santacoloma1992Santamarinafojo1992*Santaren1993  Santarius1992 Santavy1992 Santell1992I Santi1992. Santi1997YSantiago19808(Santiago1997+Santiago19981.Santiago19991 Santini19925 Santiveri2002. Santomo1999M Santoro1984\ Santoro1986) Santoro1986 Santoro19881 Santoro1988A Santoro1991 Santoro1992 Santoro1992^ Santoro1992 Santoro1992 Santoro1992 Santoro1993 Santoro1993 Santoro19933 Santoro20025 Santoro20024 Santoro2003 Santos19939 Santos199396] Santos19996^ Santos1999Santucci19930M Sanwal19933"> Sanyal1993 Sanyal1993  Sanz1993v Sanz1994v)( Sanz19977O Saouaf19844 Sap1993+w Saper1987 Saper19928F Saraf2003Saragovi1992% Sarah1992 : Saraiva1991! Saraiva19936Sarantis1992e Saraste199205 Saraste1992s Saraste1996 ' Sarfati1990$O Sarfati1993 Sarge1992 Sargent1988! Sargent1990*R Sargent19974jSarinski2003 Sarkar19900 Sarkar19919 Sarkar199221 Sarkar20012 Sarma1965!C Sarma1993j Sartor19919 Sartorelli19861 Sartorelli19891r Sarvas19922 Sarvas19921s Sarvas199398 Sarver20038M Sarver20030G Sasabe19929K Sasabe19939 Sasabe19944Sasagawa19930"Sasahara20005MSasahara20028Sasahara20033 Sasai20013[Sasakawa2002wJ Sasaki19899 Sasaki1990 ? Sasaki1990 : Sasaki19911m Sasaki19919 Sasaki1992< Sasaki1992  Sasaki19922 Sasaki19939 Sasaki1993  Sasaki1994 / Sasaki19999 Sasaoka1992 Sasaoka19935gSashital20034Sasidhar19979 Sasisekharan19633 Sasisekharan19681 Sass2000 Sassedwight19902 Sassi200273 Sassoon19984{ Sastry2002' Sather1994 bSathyanarayana1992"G Sato19900 Sato1990v# Sato19929 Sato1992v Sato19922 Sato1993h!Y Sato19939% Sato19939% Sato19931% Sato19933% Sato1993 Sato19933 Sato1993t2 Sato19951 Sato1996v)9 Sato1997v)7 Sato1997v+M Sato19981-L Sato1998- Sato19992 Sato2000,6 Sato200103 Sato20025 Sato2003\ Satoh19910= Satoh1992!E Satoh19930F Satoh1996 Satomi19939 Satou1993 Satoyoshitake1993 Satterthwait1990 Satterthwait19902 Satterthwait2001^ Sattler1990z Sattler1990* Sattler1994& Sattler19958V Sattler19955 Sattler19964 Sattler2003 * Saucier1992/ Saudan2000r3B Saudan2002 Saudek1991  Saudek1991 * Saudek199338p Saudek20020* Sauder1996 3u Sauder1996* Sauder1998 - Sauder1998 + Sauder19987V Sauder1998 + Saudou1998 E Sauer1979% Sauer1983 Sauer1983 Sauer1983  Sauer1983$X Sauer1983 Sauer1983 Sauer1983 Sauer1983F Sauer1984 Sauer1984  Sauer1984$[ Sauer1984$Z Sauer1984$Y Sauer1984 Sauer1984 Sauer1985#h Sauer1985  Sauer1985  Sauer1985 Sauer1985 Sauer1985q Sauer1986#i Sauer1986 Sauer1986 Sauer1986 Sauer1986 Sauer1986 Sauer1986#k Sauer1987#j Sauer1987$^ Sauer1987$] Sauer1987$\ Sauer19873 Sauer1988 Sauer1988 Sauer1988p Sauer1989o Sauer1989 Sauer1989 Sauer1989 Sauer1989nti1992YSantiago19808(Santiago1997+Santiago19981 Santini1992M Santoro1984\ Santoro1986) Santoro1986 Santoro1988A Santoro1991 Santoro1992 Santoro1992^ Santoro1992 Santoro1992 Santoro1992 Santoro1993 Santoro1993 Santoro1993 Santos19939 Santos19939Santucci1993"> Sanyal1993 Sanyal1993  Sanz1993v Sanz1994v)( Sanz19977O Saouaf19844 Sap1993+w Saper1987 Saper1992Saragovi1992% Sarah1992 : Saraiva1991! Saraiva19936Sarantis1992e Saraste1992s Saraste1996 ' Sarfati1990$O Sarfati1993 Sarge1992 Sargent1988! Sargent1990*R Sargent1997 Sarkar19900 Sarkar19919 Sarkar19922 Sarma1965!C Sarma1993j Sartor19919 Sartorelli19861 Sartorelli19891r Sarvas19922 Sarvas19921s Sarvas19939G Sasabe19929K Sasabe19939 Sasabe19944Sasagawa1993J Sasaki19899 Sasaki1990 ? Sasaki1990 : Sasaki19911m Sasaki19919 Sasaki1992< Sasaki1992  Sasaki19922 Sasaki19939 Sasaki1993  Sasaki1994  Sasaoka1992 Sasaoka1993 Sasisekharan19633 Sasisekharan1968 Sassedwight1990' Sather1994 bSathyanarayana1992"G Sato19900 Sato1990v# Sato19929 Sato1992v Sato19922 Sato1993h!Y Sato19939% Sato19939% Sato19931% Sato19933% Sato1993 Sato19933 Sato1993t Sato1996v)9 Sato1997v)7 Sato1997v+M Sato19981\ Satoh1991!E Satoh1993 Satomi19939 Satou1993 Satoyoshitake1993 Satterthwait1990 Satterthwait1990 Sattler1990z Sattler1990* Sattler1994& Sattler1995 * Saucier1992 Saudek1991  Saudek1991 * Saudek19933* Sauder1996 * Sauder1998 + Saudou1998 E Sauer1979% Sauer1983 Sauer1983 Sauer1983  Sauer1983$X Sauer1983 Sauer1983 Sauer1983 Sauer1983F Sauer1984 Sauer1984  Sauer1984$[ Sauer1984$Z Sauer1984$Y Sauer1984 Sauer1984 Sauer1985#h Sauer1985  Sauer1985  Sauer1985 Sauer1985 Sauer1985q Sauer1986#i Sauer1986 Sauer1986 Sauer1986 Sauer1986 Sauer1986 Sauer1986#k Sauer1987#j Sauer1987$^ Sauer1987$] Sauer1987$\ Sauer19873 Sauer1988 Sauer1988 Sauer1988p Sauer1989o Sauer1989 Sauer1989 Sauer1989 Sauer1989 T4SRQP|9ROBNMLKJ 5155 Milner, J. 1995,%Flexibility: the Key to p53 Function?e$Trends in Biochemical Sciences20 49-51t 5157Milner-White, E.J. 1988SCHELLMAN MOTIF Recurring loop motif in proteins that occurs in right-handed and left-handed forms. Its relationship with alpha-helices and beta-bulge loopsS 199503-511"Journal of Molecular Biology 5158Milnerwhite, E.J.8 19901.4-A RESOLUTION 1.8-A RESOLUTION 3-DIMENSIONAL STRUCTURE CRYSTALLOGRAPHIC REFINEMENT ESCHERICHIA-COLI FOLDED CONFORMATION PLEATED SHEETS REFINED CRYSTAL-STRUCTURE SERINE PROTEASE X RAY ANALYSIStmSituations of Gamma-Turns in Proteins - Their Relation to Alpha-Helices, Beta-Sheets and Ligand Binding Sites 2162i385-397 20 Nov"Journal of Molecular Biology 5159>8Milton, S.C.F. Brandt, W.F. Schnolzer, M. Milton, R.C.D. 1992AMINO-ACIDS COLOR TEST DERIVATIZATION GNRH PEPTIDE HEXAFLUORO 2 PROPANOL LIQUID-CHROMATOGRAPHY PITUITARY-CELLS PREDICTION SEQUENCE SPECIFICITYTotal Solid-Phase Synthesis and Prolactin-Inhibiting Activity of the Gonadotropin-Releasing Hormone Precursor Protein and the Gonadotropin-Releasing Hormone Associated Peptide Biochemistry3137 8799-8809i 22 Sep 5160,&Mimeault, M. Stpierre, S. Fournier, A. 1993voALPHA-HELICES AMINO-ACIDS BETA-TURNS BRAIN CGRP EXPRESSION HELIX-FORMING TENDENCIES PROTEINS RECEPTOR STABILITYConformational Characterization by Circular-Dichroism Spectroscopy of Various Fragments and Analogs of Calcitonin-Gene-Related Peptide& European Journal of Biochemistry 2133g927-934c 1 May` 51612,Mimura, C.S. Admon, A. Hurt, K.A. Ames, G.F. 1990The Nucleotide-Binding Site of HisP, a Membrane Protein of the Histidine Permease - Identification of Amino Acid Residues Photoaffinity Labeled by 8-Azido-ATP&Journal of Biological Chemistryo 265g32 19535-19542 15 NovHAMin Rhee, Y. Sorin, E.J. Jayachandran, G. Lindahl, E. Pande, V.S. 2004HASimulations of the role of water in the protein-folding mechanismProc Natl Acad Sci U S A 10117 6456-6461 Apr 27 KSR 51624-Minami, Y. Kawasaki, H. Suzuki, K. Yahara, I.t 1993ACTIN-FILAMENTS AMINO-ACID SEQUENCE ANTIBODIES GEL-ELECTROPHORESIS GLUCOCORTICOID RECEPTOR HSP90 MEMBRANE PURIFICATION QUANTITATION QUANTITIESJDThe Calmodulin-Binding Domain of the Mouse 90-kDa Heat Shock Protein&Journal of Biological Chemistry  26813 9604-96103 5 May9 516382Minden, J.S. Agard, D.A. Sedat, J.W. Alberts, B.M. 1989}Direct cell lineage analysis in Drosophila melanogaster by time-lapse, three-dimensional optical microscopy of living embryosJournal of Cell Biology 1092505-516 Aug 5164"Mine, Y. Chiba, K. Tada, M.  1993BETA-LACTOGLOBULIN COMPLEX EMULSION STABILITY LECITHIN LYSOPHOSPHATIDYLCHOLINE MONOLAYERS PHOSPHATIDYLCHOLINE PROTEIN CONFORMATION VESICLESEffect of Phospholipids on Conformational Change and Heat Stability of Ovalbumin - Circular Dichroism and Nuclear Magnetic Resonance Studies0*Journal of Agricultural and Food Chemistry412157-161 Feb1 5165"Mineyuki, Y. Gunning, B.E.S. 1990ALLIUM CAFFEINE CYTOKINESIS GUARD MOTHER CELLS INHIBITION PHRAGMOSOME PLATE PROTOPLASTS ROOT-MERISTEMS STOMATAL DIFFERENTIATIONiA Role for Preprophase Bands of Microtubules in Maturation of New Cell Walls, and a General Proposal on the Function of Preprophase Band Sites in Cell Division in Higher PlantsJournal of Cell Scienced97527-537 Nov 5166&Ming, Z. Lambert, H. Landry, J.l 1993Transient Activation of a Distinct Serine Protein Kinase Is Responsible for 27-kDa Heat Shock Protein Phosphorylation in Mitogen-Stimulated and Heat-Shocked Cells&Journal of Biological Chemistrya 2681  35-43 5 JanMING REGIONActivated Conformations of the ras-Gene-Encoded p21 Protein .1. An Energy-Refined Structure for the Normal p21 Protein Complexed with GDP96 1025-1044 Jun4.Journal of Biomolecular Structure and Dynamics\UDyson, H. J. Cross, K. J. Houghton, R. A. Wilson, I. A. Wright, P. E. Lerner, R. A. 1985ztThe immunodominant site of a synthetic immunogen has a conformational preference in water for a type-II reverse turn Nature 318480-483&"folding(r&#r&9r&;r&Hr&`r&yr&~r&r&r&r+Qr+Wr)6r)4rWr+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+r+rF$SJE*S(S$S(S$S$S)S%S+*S&S&S%AS%dS'(S*S+1S%S)S%S%S(S)S&S&S+S(S&BS(S'&S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+S+Ser with the locations of known epitopes, chemical modifications, and mutations. Evidence is also reviewed concerning the identity of the GTP-binding sites, about which residues are exposed in the assembled microtubule and at subunit:subunit interfaces. These characteristics constrain the possible tertiary structure of the tubulin subunit.f`alpha-Tubulin, beta-Tubulin, and gamma-Tubulins -Sequence Comparisons and Structural Constraints("Cell Motility and the Cytoskeleton203181-189Natural(l l l l' llllll*lll*klXllll!ll(l!!l#l$|l/Zl3l4l4:l6Ll6~l7ltll l l xl&ll ltlMl&lllll!l+_l+sl0l6l6 l6l6l6l6!l6Ll6l7l7+l7l7l7l7l7l7l8l4'llye& e2 e2" e  e e  e e5 e6+ e7 e8< eVe!ee ze eee}e}eNucleic Acids Research1615 7545-7562 11 Aug 4564,&Lipka, G. Denkamp, J.A.F.O. Hauser, H. 1991@9ELECTRON-MICROSCOPY PHOSPHATIDYLCHOLINE TOPOLOGY VESICLESs~xLipid Asymmetry in Rabbit Small Intestinal Brush Border Membrane as Probed by an Intl&YJ&Za&`a&da&a&wa&va&ta&|a&{a&~a&a&a&a&a&a&a&a&a'#a+Ha+Ka+La+Oa+Qa+Ta+Wa)(a))a) a+[aa+^aaaa+`ara+aa'La'Kaa+eaa)EaE)aE)aE)aE)aE)aE)a)Ea)Ea)Ea)Ea)Ea)Ea)Ea)Ea)Ea)Ea)Ea)Ea)EaI EvaluationK n n - n  n  n  n  n  n n ng n n n n8 n n n& n nL nd nc n n!p n! n$2 n$F n,) nb n, n} n.' n n4 n77 n8\ n97 n n nM na n n6z n8j n8u ndns'<e0ee:e@eBeDeeeeee e e e ePSurrey1992 Surridge1990! Surridge1992! Suss1990v%Susskind19833Susskind19833#hSusskind19855" Sussman1990 Sussman1992" Sussman1993!t Sussman1993 Sutarto1992 Sutcliffe1988  Sutcliffe1991! Sutcliffe1991 Sutcliffe1991D Sutcliffe1992! Sutcliffe1992! Sutcliffe1993 Sutcliffe1993 Suter1981! Sutherland1976? Sutherland1980 rrey1992 6 "IIG gb7bbob&b`bbbb(bbbIbLbbbb'bbbcbbnbabgbb )b b%b%b& b)%b)&b+b*bb4xb'Zb6ub7b8tb\bCbbObubAAAA VA A)A)A -A xA' AA)A7AAAAwAAA`AAAA a o) odecastillian)n Xndee)e eeee*eee+ee eee!eee xe yeb)bbb#b&b+|b+b+b}berge`eddtt3t0t tt*tDttmmmvmmmmm Ym k"x))))&&&&&&&[[[[[X[XXXXXXXXXXX'Y'Y'Y'Y'Y'Y'Y'Y'Y-----']']']']             ++++++++++++++++++///////+++++++.... S S S S S S S S S S S*h*h*h1111111111bbbbb+~*$)T(%&'!"#$  B 1486.(Cuatrecasas, P. Fuchs, S. Anfinsen, C.B. 1967pjThe interaction of nucleotides with the active site of staphylococcal nuclease. Spectrophotometric studies&Journal of Biological Chemistryr 24220 4759-4767U 25 Oct 14852+Cuatrecasas, P. Edelhoch, H. Anfinsen, C.B.S 1967ztFluorescence studies of the interaction of nucleotides with the active site of the nuclease of Staphylococcus aureus585 2043-2050 NovVOProceedings of the National Academy of Sciences of the United States of Americat 1489.(Cuatrecasas, P. Fuchs, S. Anfinsen, C.B. 1968xqThe effect of a competitive inhibitor on the acetylation of tyrosyl and lysyl residues of staphylococcal nucleaseu$Biochimica et Biophysica Acta  1592417-4190 4 Jun 14940*Cuatrecasas, P. Wilchek, M. Anfinsen, C.B. 1968F@Staphylococcal nuclease: size and specificity of the active siteScience 162o 861 1491-1493 27 Dec 14930*Cuatrecasas, P. Wilchek, M. Anfinsen, C.B. 1968>8Selective enzyme purification by affinity chromatography612636-643 OctVOProceedings of the National Academy of Sciences of the United States of America 14922+Cuatrecasas, P. Taniuchi, H. Anfinsen, C.B.l 1968PIThe structural basis of the catalytic function of staphylococcal nuclease2114172-200 Jun$Brookhaven Symposia in Biology 1490.(Cuatrecasas, P. Fuchs, S. Anfinsen, C.B. 1968lfThe tyrosyl residues at the active site of staphylococcal nuclease. Modifications by tetranitromethane&Journal of Biological Chemistryc 24318 4787-4798@ 25 Sep 14960*Cuatrecasas, P. Wilchek, M. Anfinsen, C.B. 1969zsAffinity labeling of the active site of staphylococcal nuclease. Reactions with bromoacetylated substrate analogues&Journal of Biological Chemistryu 244716 4316-4329 25 Aug 14950*Cuatrecasas, P. Wilchek, M. Anfinsen, C.B. 1969D=The action of staphylococcal nuclease on synthetic substrates Biochemistry86 2277-2284 Jun 1491.(Cuatrecasas, P. Fuchs, S. Anfinsen, C.B. 1969ZTCross-linking of aminotyrosyl residues in the active site of staphylococcal nuclease&Journal of Biological Chemistry& 244s2406-412 25 Jan 1497Cudd, A. Fridovich, I. 1982f_Electrostatic interactions in the reaction mechanism of bovine erythrocyte superoxide dismutase&Journal of Biological Chemistryu 257p19 11443-11447u 10 Oct 1498 Cuenoud, B. Schepartz, A. 1993C/EBP COILED-COIL DESIGN FOS GEL-ELECTROPHORESIS JUN LEUCINE ZIPPER PROTEINS MOTIF TRANSCRIPTIONAL ACTIVATOR PROTEIN YEAST GCN4`\VAltered Specificity of DNA-Binding Proteins with Transition Metal Dimerization DomainsScience 259c 5094510-513 22 Jan 1499F?Cuezva, J.M. Flores, A.I. Liras, A. Santaren, J.F. Alconada, A.o 1993D=ACYL-COA OXIDASE ADP-ATP CARRIER ESCHERICHIA-COLI GROEL F-1-ATPASE ALPHA-SUBUNIT HEAT-SHOCK PROTEIN MATRIX PROCESSING PROTEASE MITOCHONDRIA MOLECULAR CHAPERONES ORGANELLE BIOGENESIS OUTER-MEMBRANE PROTEIN PEROXISOMES PRECURSOR PROTEINS PROTEIN SORTING RAT-LIVER PEROXISOMES SACCHAROMYCES-CEREVISIAE YEAST MITOCHONDRIAONGMolecular Chaperones and the Biogenesis of Mitochondria and PeroxisomesIBiology of the Celli771E 47-62 1500 Cui, J.S. Somerville, R.L. 1993jcACTIVATOR EXPRESSION GENE K-12 REGULATORY PROTEINS REPRESSOR SEQUENCE SYSTEMS TRANSCRIPTION VECTORS The TyrR Protein of Escherichia-Coli, Analysis by Limited Proteolysis of Domain Structure and Ligand-Mediated Conformational Changes&Journal of Biological ChemistryU 268 7 5040-5047 5 Mar- O M@ N L H I J 2913.(Haass, C. Pesold-Hurt, B. Kloetzel, P.M. 1990JCThe Drosophila PROS-29 gene is a new member of the PROS-gene familyNucleic Acids Research1813 4018 11 Jul 2911Haass, C. Kloetzel, P.M. 1990d]Molecular analysis of alpha ecdysone induced 16S complexes in Drosophila Schneider's S3 cells:3Biochemical and Biophysical Research Communicationsl 168P1314-319 16 Apr 2909("Haass, C. Klein, U. Kloetzel, P.M. 1990TMDevelopmental expression of Drosophila melanogaster small heat-shock proteins Journal of Cell Science 96 (( Pt 3))413-418c Julo 2908(!Haass, C. Hung, A.Y. Selkoe, D.J.s 1991Processing of beta-amyloid precursor protein in microglia and astrocytes favors an internal localization over constitutive secretionJournal of Neuroscienced1112 3783-3793l Decp 2916Haass, C. Schlossmacher, M.G. Hung, A.Y. Vigopelfrey, C. Mellon, A. Ostaszewski, B.L. Lieberburg, I. Koo, E.H. Schenk, D. Teplow, D.B. Selkoe, D.J. 1992TNALZHEIMERS-DISEASE BRAIN IDENTIFICATION LOCALIZATION PRECURSOR PROTEIN TISSUESRKAmyloid beta-Peptide Is Produced by Cultured Cells During Normal MetabolismP Nature 359 6393322-3253 24 Sep 2912<6Haass, C. Koo, E.H. Mellon, A. Hung, A.Y. Selkoe, D.J. 19920*ALZHEIMERS-DISEASE IDENTIFICATION RECEPTOR}Targeting of Cell-Surface beta-Amyloid Precursor Protein to Lysosomes - Alternative Processing into Amyloid-Bearing Fragments. Nature 357 6378500-5033 11 Jun 2907HBHaass, C. Hung, A.Y. Schlossmacher, M.G. Teplow, D.B. Selkoe, D.J. 1993b\ALZHEIMERS-DISEASE CLEAVAGE IDENTIFICATION LOCALIZATION PRECURSOR PROTEIN RECEPTOR SECRETIONWe have analyzed the cellular processing pathways which produce the 4-kDa amyloid beta-peptide (Abeta) and a 3-kDa derivative (p3) of the beta-amyloid precursor protein (betaAPP) found in conditioned media of tissue culture cells and in cerebrospinal fluid. Pulse-chase experiments reveal that both peptides are secreted in parallel with soluble betaAPP (APP(s)); no precursor-product relation between Abeta and p3 was found. The protease inhibitor leupeptin did not influence the production of either peptide. In contrast, the weak base ammonium chloride (NH4Cl) showed a dose-dependent inhibition of Abeta production with less decrease in p3. A similar effect was observed using the monovalent ionophore monensin. Brefeldin A completely inhibited the generation of both peptides, indicating that proteases located in the endoplasmic reticulum or early Golgi are not sufficient for the production of the small peptides. Deletion of the betaAPP cytoplasmic domain, which removes a consensus sequence that probably mediates reinternalization, caused an increase in secretion of both APP(s) and p3 and did not abolish Abeta production. These observations suggest that completely mature betaAPP within the late Golgi and/or at the cell surface is a prerequisite for Abeta production but processing within the lysosome might not be directly required. p3 appears to derive from the 10-kDa C-terminal stub of betaAPP following secretion of APP(s).\Ubeta-Amyloid Peptide and a 3-kDa Fragment Are Derived by Distinct Cellular Mechanismsu&Journal of Biological ChemistryM 2685i 3021-3024i 15 Feb8tighter6astl'.ly3kk !k [k&ak k Vk)k [k"Ck)k&0k+lk+k6ik6k6k6k7=k8$k8@k8k8k#ktopulo l l) l/ l< l"  l"  l"  l"  l" l"# l-w l*Blbeurghrookloym ,s"s"s"s"s"s4j'manstradted8mo8mo-onM,,M3a4 a4a -aa8`22h8`3244a3a12a7=aasheffe e" c" c" c" c" cchenkoe" e" e}eo'@sspsssss u uZ u u u u u X u u u1 u  s k s  sy sThesettt t tzttttt)$tMtQtRtetvt)tttt(tXtttttt)tt#t*tltttt#t%tot~ttttttt t,t4t7tCt)t&tttt t Nt t t t t t$B$5$5$5$5$5$5$5$5$5(5*5$5$5$5*E5%5%5%5%5%5% 5%5%5%5%5%5%5%!5%&5%'5&5%25%45%35%95%65%;5*5%G5%H5%^5%\5%a5%c5'(5%r5%s5*5%5%5%5%5%5%5%5%5%5%5%5%5%5%5%5 3681JDKaarsholm, N.C. Kolstrup, A.M. Danielsen, S.E. Holm, J. Hansen, S.I. 1993b[AMINO-ACID SEQUENCE CDNA CIRCULAR-DICHROISM COWS MILK KB CELLS MEMBRANE SECONDARY STRUCTUREBs7@s7As7Bs7Cs7Ds7Es7Fs7Gs7Hs7Is7Ks7Ls7Ps7Rs7Ws7Xs7Ys7]s7]s$K%ha%ja%pa5a54a5:a5Aa5Da5Ga5Ka5Ma5^a5da5ca5`a5_a5a5a5{a5a5a5a5a5a5a5a5a1a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a6a6a6a6a6a6a6a6+a6-a6:a6;a6;a;6a6;a6;a6;ah translocates across the membrane, was extended in size. Fragments of the ompA gene ranging from 522-294 bp were ligated with the procoat gene. The hybrid proteins were inserted into the membrane and processed normally, but only in the presence of functional SecA and SecY. 0014-2956|uAlterations in the extracellular domain of M13 procoat protein make its membrane insertion dependent on secA and secY& European Journal of Biochemistry 1772c267-271Basel CH-4056, Switz.-P,BOund///D./-s00[ $11H2234 4'5566"6q6667T7m7x777,8w8889>9A3 U   !  r  uB8{Lo !!"#e$-)0[ $1H1U2223 4'4556"6q6666T7m7x73U   !   r  uB8{Lo !!"e#$-)1995.6U66D6k666)6J6Y6]6&66 (6 6!6!6"6"6#6#26)6)6#w6#6)6)6*}6&6$6$*6$6$6$6) 6$6%d6*6%6%6&6)46+d6)D6)66o6)6)6'T6+y6+6!6!6!6!6!6!6!6!6!6!6( StRuctural e) eQ e e e& e*& e. e( e) e e+  e* e* e ec e e& e e* e e5 e e^ e( e e e + e* e! e" e*% e" e# e* e*h e$; e$ e* e%d e% e&R e) e& e' e+Q e)6 e)5 e'J e K e*o e*n e( e( e( e( e( e( e( e( e( e( e"L1*r1*t1*u1+01*1,A1*1+>1+1*1&S11+1,W1+1,\1*1)1&1,n1,t1(1+1&1,1*w1,1,1,1W1V1,1,1,1,1.191,1,1,1,1,11311,1,1,1,1,1+1,1,1,1,1,1,1,1,1,1,1,11dopte1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r1r$ Understanding)% o)& o0 o5 o5 o6* o6m o6r o6u o6 o6 o6 o6 o7% o7D o7L o7f o7j o7k o7o o7 o7 o7 o7 o7 o7 o7 o7 o7 o7 o81 o8H o8] o8 o8 o8 o8 o8 oood w0 w+  w6 t6 t6P t6 t7D t7R t8E t8 t6taken7 w6wents s6 s8 r6*rappedsscribed8irablea+tectedotectedotectedotectedohttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12778129c 1526 Dahdal, R.Y. Colley, K.J. 1993APPARATUS BETA 1,4 GALACTOSYLTRANSFERASE CELLS ENDOPLASMIC-RETICULUM GLYCOPROTEINS GLYCOSYLATION PROTEIN SPANNING DOMAIN SUFFICIENT TRANSMEMBRANE DOMAINSpecific Sequences in the Signal Anchor of the beta-galactoside alpha-2,6-sialyltransferase Are Not Essential for Golgi Localization - Membran4 Structure3i s4 s) s4 s+ s4 s( s4 s4 s4 s s s_ s) s * s4 s4 s'Z s%  s%j s4 s4 s5  s s5 s3 s58 s59 s5; s5V s5` s5j s5 sT s5 s5 s5 s5 s5 s5 s5 s5 s6 s6  s6 s6 s6 s6 s64 s6Q s6a s6d s6{ s6 s6 s6 s6 s6 s6 s6 s6 s6 s tic h h himontg4X'isc7'c7'c)$cog& g+d o)F o1{' o2z' o2' o2' o2' o4A' o4' o6' k6' k6' k6!' k61' k6v' k6' k6' k6' k77' k78' k79' k7' k7' k7' k6' k8+' k8' k4'k2o%isq4jq#cq gione  i T i iJ i!C i% i% i i*6k e e)e Ve5eeeLeee7*P7+17-17.17/17017117417517717817917:17;17<17>17@17C17G17H17I17L17P17_17`17b17c17e17f17g17j17l17m17o17p17q17t17v17y17}1717171717171717171717171717171717171717171717171 core module' control. The conformational behavior of both peptides was examined using (1)H NMR spectroscopy. Chemical shift dispersion, chemical shift deviation from random coil values, sequential and long-range NOEs, and H/D amide exchange rates were compared for the two peptides. We conclude that the ensemble of oxidized and reduced core module conformations samples both nativelike 4:4 and non-native 3:5 beta-hairpin structure, and that the oxidized module samples nativelike structure for a greater f 220222n22222222t22W2H22222*2K2222262222 22R2222U222W2f22 2"*2"_2"2#.2#f2#h2$%2$*2$[2$}2$2%(2%N2%2%2&22&2'2+\2)D2227c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c7c8c8c8c8c8c8c8.c84c85c8;c8<c8Cc8Jc8Lc8Rc8Tc8Xc8fc8ic8jc8vc8wc8c8c8c8c8c8c8c8c8c3Achuko$%o 2019-2024i JAH 2676D>Golde, T.E. Estus, S. Younkin, L.H. Selkoe, D.J. Younkin, S.G. 1992ALZHEIMERS-DISEASEZTProcessing of the Amyloid Protein Precursor to Potentially Amyloidogenic DerivativesScience 255c 5045728-730 7 Feb 2679& Goldenberg, D.P. Creighton, T.E. 1983TMCircular and circularly permuted forms of bovine pancreatic trypsin inhibitor 1652407-413 5 Apr"Journal of Molecular Biology BIochemistry/? i/e i0  i0  i) i0 i0 i0 i0 i0 i0 i/ i/ i i0 i0! i0" i0& i0( i03 i02 i04 i06 i0C i0T i0U i0W i0Y i0O i/ i0] i0p i iJ i i i0v i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i# i# i  i1 i)[ i0 i0 i'N i1( i  i  i  i1HTtp01u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1$S[c c/-c1c1.c1clc0c1"c0cXc0c15c17c1;c1=c1@c1Jc1Kc1Mc1Nc1Oc1Pc1Sc1Wc1Zc1gc1hc1ic1kc1lc1mc1pc1rc1tc1~c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1cR-CLONING SECRETION TRANSFERRIN VIRUSOPJHypervariable C-Terminal Domain of Rab Proteins Acts as a Targeting Signal Nature 353l 6346769-772 24 Oct 1120B;Chazin, W.J. Goldenberg, D.P. Creighton, T.E. W:uthrich, K.t 1985Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution& European Journal of Biochemistry 1522@429-437 15 Oct=======7777777"("("("("("("("("("(OOOOOOOOOOO888888888uuuuuuuuuuuu""""""""&&&&&&&&&GGGG-t-t-t-twwwwwwwnnnnnnnnnnnn&&&&&aaa+ + )))))))%%%%%%%++++++++++'P,h,h,h,h,hJHIG91CHAIN ASSOCIATION EQUILIBRIA DYNAMICS FORCE-FIELD GLOBULAR-PROTEINS MOLECULAR MECHANICS N-MONOSUBSTITUTED AMIDES NUCLEAR MAGNETIC-RESONANCE PEPTIDESConformation-Directing Effects of a Single Intramolecular Amide Amide Hydrogen Bond - Variable-Temperature NMR and IR Studies on a Homologous Diamide Series.(Journal of the American Chemical Society 1134  1164-1173  13 Feb 2532 Gellman, S.H.i 1991AQUEOUS-SOLUTION CHAIN MOLECULES CYCLODEXTRIN ETHYL METHYL SULFIDE HYDROPHOBIC INTERACTION INCLUSION COMPLEXES MOLECULAR-STRUCTURE ROTATIONAL-ISOMERISM SIGNAL-SEQUENCE VIBRATION-SPECTRAngOn the Role of Methionine Residues in the Sequence-Independent Recognition of Nonpolar Protein Surfacest Biochemistry3027 6633-6636 9 Jul 2534.'Gellman, S.H. Powell, D.R. Desper, J.M. 1992 CRYSTAL PEPTIDES PROTEINSsVPAn Unusual Hydrogen Bonding Pattern in a Crystallographically Observed beta-TurnTetrahedron LettersN3315 1963-1964c 7 Apr 2535*$Gemmecker, G. Jahnke, W. Kessler, H. 1993(!N-15 NMR NMR-SPECTROSCOPY PROTEINRKMeasurement of Fast Proton Exchange Rates in Isotopically Labeled Compoundsb.(Journal of the American  4926LEMatthews, B.W. Ohlendorf, D.H. Anderson, W.F. Fisher, R.G. Takeda, Y. 198382Cro repressor protein and its interaction with DNA:3Cold Spring Harbor Symposia On Quantitative Biologyf47 Pt 1`427-433 4927$Matthews, B.W. Rossmann, M.G.m 1985& Comparison of protein structures 115397-420Methods in Enzymology 4919Matthews, B.W. 1985\VDetermination of protein molecular weight, hydration, and packing from crystal density 114176-187Methods in Enzymology 4918Matthews, B.W.1985-86tHAStructural basis of protein stability and DNA-protein interactionOHarvey Lectures81 33-51 .b3?2h3_,307-329JCChao, H. M. Bautista, D. L. Litowski, J. Irvin, R. T. Hodges, R. S.d]Use of a heterodimeric coiled-coil system for biosensor application and affinity purification"Journal of Chromatography BD>reviews; coiled-coil system; biosensors; affinity purification; proteins; peptides Gcn4 leucine-zipper; interhelical salt bridges; alpha-helical bundle; x-ray structure; electrostatic interactions; crystal- structure; immunoaffinity chromatography; guanidine- hydrochloride; energetic contribution; secondary structureThe two-stranded or-helical coiled-coil is now recognized as one of nature's favorite ways of creating a dimerization motif. Based on the knowledge of protein folding studies and de novo design model systems, a novel heterodimeric coiled-coil protein was synthesized. The heterodimeric E/K coiled-coil was constructed with two distinct peptides (E and K) that will spontaneously associate into a full helical coiled-coil structure in solution. Equilibrium CD, NMR and real time biosensor kinetics experiments showed that the E/K coiled-coil is both structurally (Delta G(unfold)=11.3 kcal/mol) and kinetically (K-d approximate to 1 nM) stable in solution at neutral pH. The engineered coiled-coil had been applied as a dimerization and capture domain for biosensor based applications and used in an expression/detection/affinity chromatography system. Specific test examples demonstrated the usefulness of the E/K heterodimeric system in these applications. The universality of coiled-coil as a dimerization motif in nature and our ability to design and synthesize these proteins suggest a wide variety of applications. (C) 1998 Elsevier Science B.V. All rights reserved.J. Chromatogr. B 1998 71581r*$English Review SEP 11 J CHROMATOGR B81Chapeaurouge, A. Johansson, J. S. Ferreira, S. T. 2002CFolding of a de Novo Designed Native-like Four-helix Bundle Protein)  J Biol Chem+ 27719 16478-83..11832477 JAHbhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11832477 http://www.jbc.org/cgi/content/full/277/19/16478 http://www.jbc.org/cgi/content/abstract/277/19/16478/ 11002+Chapin, S.J. Bulinski, J.C. Gundersen, G.G.l 1991<5ALPHA-TUBULIN ORGANIZATION TAU TUBULIN POLYMERIZATIONI$Microtubule Bundling in Cells Nature 349 630424 3 Jan 1098"Chapin, S.J. Bulinski, J.C.  1991ANTIBODIES BRAIN CULTURED HELA-CELLS EXPRESSION IDENTIFICATION IMMUNOFLUORESCENCE LOCALIZATION NERVOUS-SYSTEM PHOSPHORYLATION TRANSCRIPTSNon-Neuronal 210x103 Mr Microtubule-Associated Protein (MAP4) Contains a Domain Homologous to the Microtubule-Binding Domains of Neuronal MAP2 and tauJournal of Cell Sciencen98 27-36p Jani 1099"Chapin, S.J. Bulinski, J.C.i 1992~wBINDING DOMAIN BRAIN CELLS EXPRESSION MAP2 MITOTIC SPINDLE MOLECULAR CHARACTERIZATION MOUSE-TISSUES TAU-PROTEIN TUBULINlfMicrotubule Stabilization by Assembly-Promoting Microtubule-Associated Proteins - A Repeat Performance("Cell Motility and the Cytoskeleton234 236-243c 1101F@Chapman, E.R. Alexander, K. Vorherr, T. Carafoli, E. Storm, D.R. 1992LEFluorescence Energy Transfer Analysis of Calmodulin.Peptide Complexesu Biochemistry3151 12819-12825 29 DecB8Chatani, E. Nonomura, K. Hayashi, R. Balny, C. Lange, R. 2002Comparison of heat- and pressure-induced unfolding of ribonuclease a: The critical role of Phe46 which appears to belong to a new hydrophobic chain-folding initiation siteP Biochemistry41144567-74.11926818 JAHiZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11926818a.(Chatellier, J. Buckle, A.M. Fersht, A.R. 1999xGroEL recognizes sequential and non-sequential linear structural motifs compatible with extended b-strands and a-helices a b o p "Journal of Molecular Biology 292163-172 SJE Chatrenet, B. Chang, J.-Y. 1992D=The folding of hirudin adopts a mechanism of trial and error. 267 3038-3043&Journal of Biological Chemistryb)!PRotein)*+[+]++ru+_%'K+c'O'J+h+i*+l Q(&)D)+o+po'R'Q)#+{)I+O++++++++++++++++++++992%EWoolfson1993%DWoolfson1993%FWoolfson1993Woolfson1993+Woolfson19989Y Woollenweber1993%G Woolley1992%H Woolley1993: Woolley1993%I Wootan1993 %J Wooten19911* Word1998a%K Wormald1991%J Wormald1991c Wormald1992%L Worman1990 . Worman19933l Wormbreitgoff1991 |Worosila1993+> Worrall1998 Worrell1994 e Worthington1992s Wortman1984`Woudstra199N+Ofc+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N)N*N*NN+N!N*N*N*N*N*N*N*N*N*N*N*N*NNNNNNNNNNNNNX+x1998+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9+9)IsnsO{O~OOOOOOO O O .O 5O)O sO xO O O O O O O O!#O!0O!1O!3O!?O!OO!YO!bO!O!O!O"O" O" O"O*O"2O"XO"\O"bO)O"O"O*VO"O)NO*/O)WO#O#O#/O#AO#_O#O#O#O#O#O#O#O*,#/:FPVrYn[t_t]j}.ADoo+ah phoASowwww!)*,#/:FPVrYn[t_t]j}.ADoo+ah dBINDING#oO O O O O sssssscs2s/s%sssssssss #s&s*s,sasss$s(s+s-s s*ROdOactive%{chemiicals p s s s s s"Q s*'estryl lu l l i  i  i G i  i  i  i  iQ i0 i  i iw i{ i i i i i i\ i/ i i+P+2+2+2+2+2+2+2+2+2+2+2+2+2+2+2+2)2*2#U2*2+2+2,2)2*2(22+2(2+2*22+@2(2 2'`2 2(2#<2;22,2+F2+2,2,2,2+2+2+2+2+2+2+2+2+2+2+2+2+2+2+2+2Barlowe!eenn%n nas+seee]e`ee Ie e e e eeee+eeee e/eVee(eneeee(e%e%e)e Je*e+e,kee,qe,re&e)e,ue,|e#ee,e,e[Z-.=-- H..//*0122g2h2m467 78f87%folding7*r7,r7?r7Ar7Br7Cr7Er7Gr7Mr7Nr7Or7Rr7Sr7Vr7Zr7[r7\r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r82r84r8Yr8}r8r8r8r6r8r8r8r8r8r5 r)r9r9#r9%r9'r9)r9-r9/r91r9*r94r9:r99r9;r9<r9=r9?r9Ar9Br9Er9Lr9&r9Rr9,r9Sr7r*r*r7\r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r7r82r84r8Yr8}r8r8r8r8r6r8r8r8r8r8r5 r)r9r9#r9%r9'r9&r9)r*r*rmature\X`EEEE}E<EEoErEqEpEEWEEEE)E)EEEEEE EEEEEEEEEE"ELEMEcEEEEEJEE!E" E"qE"E*BE$E#E$E$ E)E$~E$E%E%E%E%E%E%E&E&E'Conversion of Insulin Units to SI Units,&American Journal of Clinical Nutrition585@714-715 Nov 8208Volz, K. Matsumura, P. 1991BACTERIAL CHEMOTAXIS CHAIN FOLDED CONFORMATION MACROMOLECULAR STRUCTURES PHOSPHOTRANSFER PROTEIN-PHOSPHORYLATION RESPONSE REGULATOR TRANSDUCTIONLFCrystal Structure of Escherichia-Coli CheY Refined at 1.7-A Resolution&Journal of Biological Chemistry  26623 15511-15519i 15 Aug6/Vonahsen, O."Acidy#T#T#T#T##T#MT#uT#T#T#T$5T$8T$JT$MT$PT$T$T$T$T%T%IT%wT%xT%{T%T%T& T+T&8T&;T&IT&HT&TT&VT&bT&uT&T+HTHT+T8T+T!T*T(T(T T'`T(T T RT(T(T,&T+-T+,T+,T+,T+,T+,T+,T+T&^unfolda,a6a6a7ja8ga ase5 eediiiiiQi*iBiDiHiWiVii i 5i ti Oi ]i iii"i%iiiiiijiVi}ii(itii>iGiiii i"i$i$i%yi%i%i&i&i+i+i+i*i,.i,5i i,@i*i,i,i2CIrcularyttttttttt&t%t,tttttt t`tttt%ttt3tKtMtLtttt^ttt t!ttt t 8t t!t!1t!Kt!^t!]t!_t!ct!kt!zt!t!t!t"Rt"St"ht"t"t"t"t"tssier1991)  Bost1995v Bost19966)T Bost1997v Boswell1988 Boswell1988A Boswell1989C Botella1991 Boteva1991 I Bothamley1992d Bothnerby1992Y Botquin1996OBotstein1983PBotstein1984Botstein1985Botstein1992 Bottaro1993Bottazzo19933 Botterman1992. Botti1999,A Botto1998+ Bottomley1992 Botuyan1996/]Bouchard2000 Boucher1992  . / - 6 2886Gupta, R.S. Singh, B. 1992DNAK GENE ESCHERICHIA-COLI EUKARYOTIC NUCLEUS EXPRESSION HEAT-SHOCK PROTEINS MEMBER NUCLEOTIDE-SEQUENCE ORIGIN RIBOSOMAL-RNA SEQUENCES SIMILARITY SEARCHES h bHeat shock induces the synthesis of a set of proteins in Halobacterium marismortui whose molecular sizes correspond to the known major heat shock proteins. By using the polymerase chain reaction and degenerate oligonucleotide primers for conserved regions of the 70-kDa heat shock protein (HSP70) family, we have successfully cloned and sequenced a gene fragment containing the entire coding sequence for HSP70 from H. marismortui. HSP70 from H. marismortui shows between 44 and 47% amino acid identity with various eukaryotic HSP70s and between 51 and 58% identity with its eubacterial and archaebacterial homologs. On the basis of a comparison of all available HSP70 sequences, we have identified a number of unique sequence signatures in this protein family that provide a clear distinction between eukaryotic organisms and prokaryotic organisms (archaebacteria and eubacteria). The archaebacterial (viz., H. marismortui and Methanosarcina mazei) HSP70s have been found to contain all of the signature sequences characteristic of eubacteria (particularly the gram-positive bacteria), which suggests a close evolutionary relationship between these groups. In addition, detailed analyses of HSP70 sequences that we have carried out have revealed a number of additional novel features of the HSP70 protein family. These include (i) the presence of an insertion of about 25 to 27 amino acids in the N-terminal quadrants of all known eukaryotic and prokaryotic HSP70s except those from arcbaebacteria and the gram-positive group of bacteria, (ii) significant sequence similarity in HSP70 regions comprising its first and second quadrants from organisms lacking the above insertion, (iii) highly significant similarity between a protein, MreB, of Escherichia coli and the N-terminal half of HSP70s, (iv) significant sequence similarity between the N-terminal quadrant of HSP70 (from gram-positive bacteria and archaebacteria) and the m-type thioredoxin of plant chloroplasts. To account for these and other observations, a model for the evolution of HSP70 proteins involving gene duplication is proposed. The model proposes that HSP70 from archaebacteria (H. marismortui and M. mazei) and the gram-positive group of bacteria constitutes the ancestral form of the protein and that all other HSP70s (viz., other eubacteria as well as eukaryotes) containing the insert have evolved from this ancient protein.Cloning of the HSP70 Gene from Halobacterium-Marismortui - Relatedness of Archaebacterial HSP70 to Its Eubacterial Homologs and a Model for the Evolution of the HSP70 GenedJournal of Bacteriology  174s14 4594-4605 Jul8 2883,&Gupta, H.M. Talwar, G.P. Salunke, D.M. 1993AMINO-ACID SEQUENCE ANALOGS ANTAGONIST CONFORMATION DECAPEPTIDE ENERGY EXPRESSION LHRH PATTERN-RECOGNITION PROTEINS RECEPTOR BINDING SITE RECEPTOR-BINDING STRUCTURE ACTIVITY DATA BASEeA Novel Computer Modeling Approach to the Structures of Small Bioactive Peptides - The Structure of Gonadotropin Releasing Hormone161 48-56 May 0*Proteins: Structure, Function and Genetics 2882Gupta, A. Chauhan, V.S. 1993ALAMETHICIN FRAGMENTS CONSTRAINED PEPTIDES DEHYDROAMINO ACIDS DEHYDROPHENYLALANINE MAGNETIC-RESONANCE NMR PROTONS SOLUTION CONFORMATIONrConformation of Dehydropeptides - Synthesis and Solution Structure of Model Peptides Containing (E) and (Z) Dehydroaminobutyric Acid Residues<5International Journal of Peptide and Protein Research415a421-426 May7r Biological7y s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s8$ s8@ s8A s8E s8H s8N s8l s8v s8w s8 s# s sf s) l+  l& l& l l l- l l l lo l  l# l$ l)' l+y l5 l5 l6! l63 l6L l6N l6\ l6{ l6 l6 l6 l6 l7 l7 l79 l7K l7 l7 l7 l7 l7 l7 l7 l7 l7 l8 l8? l8A l8P l8U l8] l8{ l8 l8 l8 l)) l+X l'O l+ l+ l+ l+ l+s l)/ l1I' l1N' l1Y' l1g' l1|' l1}' l1}' l1}' l5 l5 l!6 l36 lL6 lN6 l\6 l{6 l6 l6 l6 l6 l7 l7 l97 lK7 l7 l7 l)) lX+ lO' l+ l+ l+ l+ ls+ l/) lI1' lN1' lY1' lg1' l|1' l}1' l|!mPTSH H H HHUtU8!ubE ERAl7?ica1'a1'a6'aation s6 l7 s7 l8 l+^lysdsheddC i i i"Z i# i$V i&7 i+ i iR i5 r6# r7% r7x r7 r8; r8^ r8 r!5 rs0j i0 i/ i9 i5 i) i" i= ing4-Med4,C4+C4*C4(C4'C4&C42C43C48C47C46C45C44C4;C4HC4GC4FC4EC4DC4CC4?C4AC4@C4>C4<C3Ofc3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N3N4N4N4N4N4N4 N4 N4 N4 N4N4N4N4N4N4N4Npmartinneeeeeeee eeeeeeeeewe ,e$e(e$ehe/e1Xe2ye3Be3e3e4e(e5=e5e7Se7e8ze8e9e e4r'e4'e4'eXeauh y  z  zzxm|m m m%c#vc-c2wc+c5}c7c7 c9Xc\carrion[s2s salas0houmouto1='sried1B' 1[' 2' 2' 2' 2' a#`a#ca#qa#~a#a#a#a)a$Oa$Ua$a$a$a$a%a% a% a%a%a%a%Da%Na%ra%ra%ra%ra%ra%ra%ra%ra%ra%raand Departments of Medical Genetics, Biochemistry and Chemistry, University of Toronto, Toronto, Ontario, M5S 1A8 Canada. 11457242 J Am Chem Soc 2001 123194556-66.ZSSlack, J. McMahan, C.J. Waugh, S. Schooley, K. Spriggs, M.K. Sims, J.E. Dower, S.K.w 1993voIndependent binding of interleukin-1 alpha and interleukin-1 beta to type I and type II interleukin-1 receptors&Journal of Biological ChemistryC 268`4 2513-2524d 5 Feb 73282AbsTRACT2t2t2t2t2t2t2t3t3t3t3 t3/t34t3:t3@t3>t3Ot3Rt3t3ct3bt3at3`t3_t3^t3]t3\t3Yt3Wt3lt3rt3mt3qt3wt3st3{t3}t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t3t12t3it52t58t8!t8t8t8t8"t1='teilung1]' u1u' u2' u6z' u7' u8' uunndancecW c c c ct_3t^3t]3t\3tY3tW3tl3tr3tm3tq3tw3ti3ts3t{3t}3t3t3t3t3t3t3t3t3t3t3t3t3t3t=1'teilung]1' uu1' u2' uunndancecW c c4 chaperone s+  s) s  s& sn s s s s sD sF s^ s s) sG sX s1 s s s 4 s( s*A s"C s"b s#+ s#, s#z s) s$ s$/ s$ s% s% s% s&. s&{ s& s+ s, s, s, s, s, s* s, s& s&} s, s  s s-} s- s.? s s. s. s. s/# s/* s/* s/* s%$   ﻯﯿ" ꧯ$ %(¨! !! %ǧ " "! $ %믾ﯽ*( 퀀! ( 󥥀( % (Complex 1e :e ?e De Me e e e e!e!Ne!Qe!e*(e!e!e!e"0e"_e"be#e#Qe#ze#e$-e$2e$ne$ze$e$e$e$e$e) e$e$e$e%e%e%9e%ae%{e%e%e%e%e&e&e&>e&Le&e&e+Xe* e)De)eeeee,e,ceSPERM WHALE MYOGLOBIN SYNTHETIC ANTIGENIC SITE6 Abaza, M.S.I. Atassi, M.Z. 1992AMINO-ACID SUBSTITUTION FREE SYNTHETIC PEPTIDE GENETIC-CONTROL IMMUNE RECOGNITION IMMUNOGENS LYSOZYME MIMICKING MONOCLONAL-ANTIBODIES MYOGLOBINS PRECISE DETERMINATION PREDETERMINED SPECIFICITY RESIDUES SPERM WHALE MYOGLOBIN SURFACE REGIONS SYNTHETIC ANTIGENIC SITEEffects of Amino Acid Substitutions Outside an Antigenic Site on Protein Binding to Monoclonal Antibodies of Predetermined Specificity O+ Nlm11S13S14S15S16S17S18S19S1:S1;S1<S1=S1?S1@S1AS1BS1CS1DS1ES1FS1HS1IS1JS1KS1LS1MS1NS1OS1PS1QS1RS1SS1TS1US1WS1XS1YS1ZS1[S1\S1]S1^S1_S1`S1aS1bS1cS1dS1eS1fS1gS1hS1iS1kS1lS1mS1nS1oS1oS1oS1oS1oS1oSonnecting to host... Client message sent The Host closed the connection. Retrieving references 61 - 63... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Aborted Aborted Connecting to host... Connecting to host... Searching for: [Witt+SN*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the cCanaaazaa)$aRaea)aaa)a*aaaaCaa!Da!a!a"ua"xa"wa"ya"a#qa#za#{a#a#a$Ua$a)a)'a)6a)1a))a+a+^a+ha)a+oa)2a+yaOa,a-a!;a'Sa+ta+Ya+sa0a#aa)/a0a0a=a+ azazaidues in tandem binding'>8Ontario Cancer Institute, University of Toronto, Canada.9691278 J Biomol NMR 1998113307-18.orted Aborte,69691278 ArrowsmithCDdbdoptEEntrezformGardnergovHhtbinhttpKKayLm MuhandiramncbinihnlmpostqueryRrShanSubunituidwwwXɄ Subunit-spec backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a role for N-terminal residues in tandem bindinf , Ellis1988} Ellis19904 Ellis19903 Ellis19902 Ellis1990 Ellis1990 Ellis19907 Ellis19916 Ellis19919 Ellis19918 Ellis1991 Ellis1991 Ellis1991 Ellis1992; Ellis1992: Ellis1992< Ellis1993? Ellis1993> Ellis1993= Ellis1993J Ellis1993B Ellis1994A Ellis1994-z Ellis1996+W Ellis1998, Ellis19997 Ellis1999/ Ellis20002{ Ellis20007A Ellis20000 Ellis20017 Ellis20015r Ellis20037 Ellis20038 Ellis2003C Ellman1959D Ellman1992  Ellman1993 8 Ellman1999E Elmasdouri1992  Elmasry19930 elMasry1993+ ElMasry1994+ ElMasry1994C Elove1990F Elove1992%a Elove1993* Elove1997 Elovson1988 Elve1988 Elve19962 Elve2000- Elrod1999I Elsaghier1992 Elsas1992&O Elsayed1993 Elsebae1993J Elsenberg1989" Elson1971" Elson1972 Elson1988 Elson1989! Elson1991R Elson19922 Elston2002 K Eltayar1992-jElThaher19979 Elthon1993 u Elvin1991L Elwell1977 M Elwell1979 , Ely199217 Ely20012 Ely20011. Emanuelsson2000N Ember1990 Emde19939 Emerman1993 Emerson1992 Emerson1992# Emerson1993 Emi19935b Emi20034yEmmerich2002l4 Emmerling2002 Emmermann1993. Emmert1998.> Emmett1998!` Emmons19939 Emory1992 Emory1992O Emr1978 Emr1978 Emr1979R Emr1980 i Emr1980Q Emr1980P Emr1980 Emr1981S Emr19810 Emr1982V Emr1982U Emr1982T Emr1982W Emr1983 Emr1990#o Emr1990u Emr1990 Emr1991 G Emr1991 H Emr1991 | Emr1991 Emr1991v Emr1991 Emr1992! Emrick19921 Emsley1991 X Emsley1991  Emslie1992 u Emtage19877Y Emtage1993 Z Encinas1993 End1993[ Endo1987v] Endo1991v\ Endo1991v^ Endo1992v Endo19929( Endo19955) Endo199696j Endo20001K Endo200108X Endo20033_ Endow1992 Endow1993, Endres199896p Endres19989) Enenkel1995+ Enenkel1998 & Enfors19909L Enfors19911 Engberts1990 Engberts1992Engberts1993 Engel1979a Engel1991` Engel1991 @ Engel1992b Engel1992 Engel1993 Engel1993 Engel1993 Engel19940 Engel20005^ Engel2003  Engelborghs1990 Engelborghs1992 Engelbrecht1996+^ Engelbrecht1997c Engelhard1995d Engelhard1996,! Engeli19989R Engelke1993eEngelman1981$$Engelman19877%Engelman19919 Engelman1992Engelman19929Engelman1992Engelman19922Engelman1992"cEngelman19922Engelman1992 Engelman1993Engelman19969+0Engelman19986Engelman1998-Engelman19996SEngelman19996TEngelman2000 Engelmann1991f Engels1992 # Engels1992( Engels1997r2+ Engels2001r( Engen1997- Engen1999.2 Engen19998 Engen2001g Engh19921 Enghild19924^ England2002 Englander1972. Englander1978. Englander1978g Englander1980g Englander1980h Englander1984.z Englander1985.z Englander1985# Englander1986i Englander1987 Englander1988  Englander1989# Englander1989C Englander1990  Englander1990  Englander1990  Englander1990# Englander1990 Englander1990j Englander1991j Englander1991F Englander1991  Englander1991l Englander1992k Englander1992k Englander1992q Englander1992E Englander1993n Englander1993 Englander1993< Englander1993I Englander1994H Englander1994 + Englander1994& Englander1995& Englander1995L Englander1995 Englander19951993B Ellis1994A Ellis1994z- Ellis1996W+ Ellis1998, Ellis1999/ Ellis2000{2 Ellis20000 Ellis2001C Ellman1959D Ellman1992  Ellman1993 E Elmasdouri1992  Elmasry19930 elMasry1993+ ElMasry1994+ ElMasry1994C Elove1990F Elove1992a% Elove1993* Elove1997 Elovson1988 Elve1988 Elve19962 Elve2000- Elrod1999I Elsaghier1992 Elsas1992O& Elsayed1993 Elsebae1993J Elsenberg1989" Elson1971" Elson1972 Elson1988 Elson1989! Elson1991R Elson19922 Elston2002 K Eltayar1992j-ElThaher19979 Elthon1993 u Elvin1991L Elwell1977 M Elwell1979, Ely199271 Ely20012 Ely2001.1 Emanuelsson2000N Ember1990 Emde19939 Emerman1993 Emerson1992 Emerson1992# Emerson1993 Emi1993 Emmermann1993. Emmert1998>. Emmett1998`! Emmons19939 Emory1992 Emory1992O Emr1978 Emr1978 Emr1979R Emr1980i Emr1980Q Emr1980P Emr1980 Emr1981S Emr19810 Emr1982V Emr1982U Emr1982T Emr1982W Emr1983 Emr1990o# Emr1990u Emr1990 Emr1991G Emr1991H Emr1991| Emr1991 Emr1991v Emr1991 Emr1992! Emrick19921  Emsley1991 X Emsley1991  Emslie1992 u Emtage19877Y Emtage1993 Z Encinas1993 End1993[ Endo1987v] Endo1991v\ Endo1991v^ Endo1992v Endo19929( Endo19955) Endo19969K1 Endo20010_ Endow1992 Endow1993, Endres19989) Enenkel1995+ Enenkel1998& Enfors19909L Enfors19911 Engberts1990 Engberts1992Engberts1993 Engel1979a Engel1991` Engel1991@ Engel1992b Engel1992 Engel1993 Engel1993 Engel1993  Engel19940 Engel2000  Engelborghs1990 Engelborghs1992 Engelbrecht1996^+ Engelbrecht1997c Engelhard1995d Engelhard1996!, Engeli19989R Engelke1993eEngelman1981$$Engelman19877%Engelman19919 Engelman1992Engelman19929Engelman1992Engelman19922Engelman1992c"Engelman19922Engelman1992 Engelman1993Engelman199690+Engelman1998-Engelman1999 Engelmann1991f Engels1992 # Engels1992( Engels1997r+2 Engels2001r( Engen1997- Engen19992. Engen1999g Engh19921 Enghild1992 Englander1972. Englander1978. Englander1978g Englander1980g Englander1980h Englander1984z. Englander1985z. Englander1985# Englander1986i Englander1987 Englander1988  Englander1989# Englander1989C Englander1990  Englander1990  Englander1990  Englander1990# Englander1990 Englander1990j Englander1991j Englander1991F Englander1991  Englander1991l Englander1992k Englander1992k Englander1992q Englander1992E Englander1993n Englander1993 Englander1993< Englander1993I Englander1994H Englander1994+  Englander1994& Englander1995& Englander1995L Englander1995r1995G, Vlassi1999 Vlasuk19922 y Vo199392 Vo2002a% Vockley1992 Voellmy1992 Voellmy1993# Vogel1984# Vogel1990 Vogel1992# Vogel1992# Vogel1992 Vogel1992 Vogel1992 Vogel1993&J Vogel1993 Vogel1993 Vogel1993# Vogel1993$ Vogel1993& Vogel1993! Vogel1993+s Vogel1994) Vogel1998, Vogel19986p Vogel1998/ Vogel20000 Vogel2001 Vogelstein1992 + Vogl1997@) Vogt199598Vogtherr2002o# Voigt1993. Voisine1999/ Voisine1999( Volanakis1992# Volarevic19930 Volchuk2000#n Volckaert1991x Volckaert1993* Vold1997vR Volger1996 " Volke1990Z Volkenstein1986# Volkenstein1991# Volker1991 # Volker1991 ' Volker1992$ Volker19929 Volker199390 Volkert1999 Volkin1993 q Volkin1993 2 Volkin1995<D Volkman1992/ Volkman19997 Volkman20018J Volkman2003%Volkmann199334 Volkmer20020rVolkmer-Engert20013lVolkmer-Engert2001& Volknandt19937 Volkov19988`Volkwein1996j Voltattorni1993# Volund1993 , Volwerk1985, Volwerk1988# Volz1991v Volz19929/ von Ahsen19996a von Bergen2002 [ von der Haar19768| Von Der Mulbe2002# von Heijne1985# von Heijne1988# von Heijne1989 Von Heijne1990 # von Heijne1990# von Heijne1991# von Heijne1991# von Heijne1991# von Heijne1991# von Heijne1992# von Heijne1995/7 von Heijne1996) von Heijne1996). Von Heijne1997 )@ von Heijne1997+^ von Heijne19977+h von Heijne1997)0 von Heijne1997* von Heijne1998 0 von Heijne19986~ von Heijne19986 von Heijne1998/6 von Heijne1999L0 von Heijne20001. von Heijne200007 von Heijne200118 von Heijne2003. von Hippel1989) von Hippel1997 6 von Hippel1997 von Jagow1987 von Jagow19877 von Knoblauch20024von Knoublauch2002d#Vonahsen1995 Vonbonsdorff1992 | Vonderhaar1991 # Vonderviszt1990# Vonderviszt1992# Vonderviszt1992Voneckardstein1993&Voneuler19933$Vonfeldt19911 Vonfigura1991 Vonfigura1992' Vonfigura1993 Vonfigura1993 ) Vonfigura1993$G Vonfreyberg1991%l Vonfreyberg1991 Vongabain1993  Vonheijne1990 Vonheijne1991  Vonheijne1991 Vonheijne1992R Vonheijne1992 Vonheijne1992 Vonheijne1993 Vonheijne1993f Vonheijne1993 Vonheijne1993 Vonheijne1993$ Vonheijne1993$ Vonheijne1993 Vonheijne1993 Vonheijne1994 Vonheijne1994 Vonheijne1994  Vonheijne1994$ Vonheijne1995) Vonheijne1995) Vonheijne1995) Vonheijne1996$ Vonheijne1996 Vonheijne1996# vonHippel1964  Vonhippel1993 Vonhippel1993# vonHippel1994 Vonjagow19929 Vonkieckebuschguck1992#Vonkries1991${Vonphilipsborn1992 Vonruden19933& Vonschaewen1992TVonwilckenbergmann1993,Voordouw1992 Voorhees19933 Voorhees1993 Voorhorst1990/ Voornbrouwer1992 Voorter1993 Voos1990# Voos1993v Voos19939 T Voos19939# Voos19951/ Voos199992 Voos200007= Voos200001C Voos200101X Voos200103 Voos20022# Vordermark1990 1iVorderwulbecke20017'Vorderwulbecke20025Vorderwulbecke20038Vorderwulbecke2003l49Vorderwlbecke2002 Vorherr1992# Vorherr1992# Vorherr1993 Vornhagen19939Vorontsov-Velyaminov1992 Vos19926 Vos2000 w Voss19900! Voss19929# Voss1993 Vossebeld19924Voulhoux2003o Vovelle19928 Voyer2003/ Vranken19994 Vranken2002 Vrieling1993)Vrielink19958Vrielink2003r# Vriend1990  Vriend19922 Vriend19922 Vriend1992  Vriend1993 -: Vriend199998C Vriend20030 v Vrona19920 Vrontou19990 Vrontou20013 Vrontou2002# Vtyurin19933w Vu20014G Vu20022 Vucelic1992/ Vugmeyster200086 Vugmeyster2000 E Vuilleumier1992# Vuilleumier1993# Vuilleumier1993+ Vuilleumier1995,r Vuilleumier1996# Vuister1990# Vuister1991# Vuister1992# Vuister1992# Vuister1992# Vuister1993# Vuister1993# Vuister1993# Vuister1993# Vuister1993$ Vuister19940 Vulcu2001# Vulliet1992* Vunnam1998 Vuong1993 Vuong1993# Vuori1992# Vuori1992# Vyas1993v W:uthrich1985 Wabl199395 Wach1991"q Wachter1990 Wachter1991& Wachter1991$ Wachter1991 Wachter1992# Wachter1992 ! Wachter19936 Wachter1997# Wada1981v# Wada1982v Wada19839!y Wada19858 Wada19868# Wada1986 Wada19899K Wada19901# Wada1991v, Wada19921 Wada19929 Wada19929L Wada19921 Wada19922# Wada1992v Wada19921U Wada19931 Wada19933!_ Wada199394} Wadai2002 Waddell1985 Waddon19944 Wade19929 Wade19939# Wade1993v# Wade1993v& Wade19959*: Wade19977, Wade199770& Wade20000&2 Wadsworth1990 Wadsworth1993# Waegemann1991  Waegemann1992"GWaelchli1990 Wagenaar199197Wagenknecht-Wiesner2003!Waggoner1989# Waghorn19841- Wagner( Wagner1979  Wagner1981 # Wagner1982  Wagner1983* Wagner19888* Wagner1991 Wagner1991  Wagner19911 m Wagner1991s  Wagner19929b Wagner1992 Wagner19922 Wagner19922# Wagner1992  Wagner1992  Wagner1992 z Wagner19929 Wagner19929M Wagner19922# Wagner1993 # Wagner1993 # Wagner1993+ Wagner19933+ Wagner19939+ Wagner1993+ Wagner19939# Wagner1994  Wagner1994 Wagner1994 + Wagner19949+ Wagner19941'X Wagner1995  Vuilleumier1993# Vuilleumier1993+ Vuilleumier1995# Vuister1990# Vuister1991# Vuister1992# Vuister1992# Vuister1992# Vuister1993# Vuister1993# Vuister1993# Vuister1993 Vuong1993 Vuong1993 W:uthrich1985 Wabl19939"q Wachter1990 Wachter1991& Wachter1991$ Wachter1991 Wada19839!y Wada19858 Wada19868 Wada19899K Wada19901# Wada1991v, Wada19921 Wada19929 Wada19929L Wada19921 Wada19922# Wada1992vU Wada19931 Wada19933!_ Wada19939 Waddell1985 Waddon19944 Wade19929 Wade19939# Wade1993v# Wade1993v& Wade19959&2 Wadsworth1990 Wadsworth1993# Waegemann1991  Waegemann1992"GWaelchli1990 Wagenaar19919# Waghorn1984( Wagner1979 # Wagner1982 * Wagner19888* Wagner1991 Wagner1991  Wagner19911  Wagner19929b Wagner1992 Wagner19922 Wagner19922# Wagner1992  Wagner1992  Wagner1992 # Wagner1993 # Wagner1993 # Wagner1993# Wagner1994  Wagner1994'X Wagner1995 Xv Christophe1993 a Christova1993G Christy1982/ Chrivia19930 Chrunyk1993" Chrunyk19937- Chrunyk19947E Chrunyk1994 Chrusciel1991 Chrusciel19923mChrysina2001* Chu119807 Chu19881 Chu19912 Chu1992$M Chu19924 Chu19933 Chu1993. Chu1999/ Chu19996 Chu19992 Chu20001 Chu20023 Chu20023 Chu2002 Chuang1992 %w Chuang1992 5 Chuang1992 % Chuang199396 Chuang1993 %{ CHuang1994 3 Chuang20024 Chuang20037 Chuang2003^ Chugani1991" Chuman19919 Chung1991Z Chung1991 Chung1991%2 Chung1992&u Chung1992 Chung1992r Chung1993% Chung1993 Chung1996 Chung1996( Chung1997/= Chung1997) Chung1998+L Chung1998.1 Chung1999/ Chung2000/ Chung20000 Chung20001 Chung20014s Chung20029^ Chung2003 Chupin19955)  Chupin1995 )  Chupin1995 )Churcher1993 Churchich1993* Churchich1993 Churgay1993 Churgay19931 Chute1999c Chyan19928s Chyba20018r Chyba2002 Chytil1975 Chytil1975  Chytil1976  Chytil1976  Chytil1976  Chytil1978  Chytil1978 !X Chytil1979 7 Chytil1979  Chytil1979  Chytil1980 \ Chytil1981 + Chytil19811 Chytil1981  Chytil1982  Chytil1983 8 Chytil1983 9 Chytil1984 : Chytil1985 ; Chytil1986 = Chytil1987 < Chytil1987  Chytil19881? Chytil1994 +V Ciammaruconi19981 Ciani20016 Ciani2002 Ciardelli1990  Ciardelli1991 Ciardelli1991 Ciardelli1991 Ciardelli1993  Ciechanover1991, Ciechanover19988 Cieplak19953 Cieplak20024 Cieplak2003 X Cierniewski19934 Cierpicki20014 Cierpicki2002@ Ciesla1991 A Cieslar1988 Cieslar1989 Cieslar1989 P Cieslar1990( Cieslar1991J Cieslar1993 Cieslar1993 v Ciliberto1992Q Cines1992B Ciocca19920 Ciofi-Baffoni2001C Cioni19933{ Cioni20026 Cirilli2001 Ciriolo1993 Ciruela1992D Cistola1989E Cistola1990: Cistola1990& Cistola1991( Cistola1995  Cistola1995F Cistola1996 Cistola1996 Cistola1996'` Cistola1997& Cistola1997+; Cistola1998. Cistola1998-; Cistola1999G Citron1992  Ciurak1993i. Civera19996 Civera19996i Civera20000 Civin19920Clackson2000H Cladera1992%  Claessens1990< Claeyssens1989  Claeyssens1992 & Clagettdame1993I Clairmont1992. Clakre19999*" Clancy1989 Clanton1992J Clapham1993 Clapham1993 Clardy19922/ Clardy199887 Clare20038Clarimon2003K Clark1990 Clark1990 Clark1991L Clark1991M Clark1991& Clark1992$ Clark1992% Clark1992B Clark1992P Clark1992O Clark1992N Clark1992 Clark1993 Clark1993  Clark19936 Clark1993 5 Clark1993  Clark1993# Clark1993Q Clark1993-/ Clark1995T Clark1996( Clark1997) Clark1997) Clark1997& Clark1997) Clark19986 Clark1998, Clark1999, Clark1999/ Clark20009> Clark20013< Clark20023 Clark20024 Clark20025o Clark20037 Clark-Lewis19948] Clark-Lewis2003U Clarke1989  Clarke1990- Clarke1990 V Clarke1990  Clarke1991 8 Clarke19919 Clarke199293 Clarke1992 Clarke19921X Clarke1992W Clarke1992 ^ Clarke19933Y Clarke1993 ] Clarke1993 \ Clarke1993 [ Clarke1993 Z Clarke1993  Clarke19939 Clarke19939 Clarke19933 f Clarke19939 Clarke19939 , Clarke19939] Clarke19933 Clarke199390M Clarke1993` Clarke1994 h Clarke19949 Clarke19944 Clarke19955= Clarke19955-m Clarke19955b Clarke1996 * Clarke199693t Clarke199663 Clarke19966& Clarke19979( Clarke1997 * Clarke19977( Clarke1997 ( Clarke1997+ Clarke19971 Clarke1997<2) Clarke1997<3o Clarke19977) Clarke1998 ) Clarke1998 * Clarke19989) Clarke1998 ) Clarke19988.L Clarke199847 Clarke19988- Clarke1999 - Clarke19999. Clarke1999. Clarke1999/{ Clarke199990) Clarke199993 Clarke19999/ Clarke20000/ Clarke20000/ Clarke200001 Clarke20002& Clarke2000<2h Clarke2000<3v Clarke200003 Clarke200003 Clarke200003 Clarke200002' Clarke2001<2( Clarke200116 Clarke20011 Clarke200223H Clarke200223^ Clarke2002247 Clarke2002a4I Clarke200204 Clarke20035W Clarke20035 Clarke200339j Clarke200553Clarkson20022 Claudio19932 Clausen2002$K Clausmeyer1992 4Claverie2001 Claxton1993 3 Clayton1991c Clearwater1991 Clegg1992d Clegg1993*9 Clegg1997f Cleland1992e Cleland1992'S Cleland1997 Clemens1992 Clemens1993+L Clemens1998Q Clement1980 Clement1981h Clement1992/Clementi20002YClementi2000w2\Clementi2001w6Clementi2003i Clemetson1992i Clemetson1992+  Clemons1998. Clemons19997f Clemons19998 Clemons2004 Clerc1993/ Clerico20003 Clerico2001Clericus19939. Cleve1999j Cleveland1991&e Cleveland1991 Cleveland1992 Cleveland19920g Cleverley20014| Cleverley2002#! Clevers1993 Click1993/{ Cliff19993 Cliff20003^ Cliff2002Clifford1991 Cline1990 Cline1991k Cline1993% Cline1993$R Cline1994)) Cline1997+{ Cline1997l Cload1993& Cload1996 Cloney1990 n Cloney1992 m Cloney1992 o Clore1982p Clore1983,S Clore1987q Clore1988W Clarke1992 ^ Clarke19933Y Clarke1993 ] Clarke1993 \ Clarke1993 [ Clarke1993 Z Clarke1993  Clarke19939 Clarke19939 Clarke19933 f Clarke19939 Clarke19939 , Clarke19939] Clarke19933 Clarke19939` Clarke1994 h Clarke19949 Clarke19955= Clarke19955b Clarke1996 * Clarke19969& Clarke19979( Clarke1997 * Clarke19977( Clarke1997 ) Clarke1998 ) Clarke1998 * Clarke19989) Clarke1998 *~ Clarke19988) Clarke19988$K Clausmeyer1992  Claxton1993 3 Clayton1991c Clearwater1991 Clegg1992d Clegg1993*9 Clegg1997f Cleland1992e Cleland1992'S Cleland1997 Clemens1992 Clemens1993Q Clement1980 Clement1981h Clement1992i Clemetson1992i Clemetson1992+  Clemons1998 Clerc1993j Cleveland1991&e Cleveland1991 Cleveland1992 Cleveland1992#! Clevers1993 Click1993Clifford1991 Cline1990 Cline1991k Cline1993% Cline1993$R Cline1994)) Cline1997l Cload1993& Cload1996 Cloney1990 n Cloney1992 m Cloney1992 o Clore1982p Clore1983q Clore1988Clore1988" Analysisb" t";t"?t"Bt"Lt"`t"_t"t"t"t"t"t#t#t#At#_t#tt#ut#~t#t#t$t$/t$_t$`t$t$t$t$t$t$t$t$t%;t%t%t&t&)t&Bt&Ht&t&tt&t)+tt'Tt+ytUt,t-tt,tt ttt+Yt/t/t/t/t/t/t/t/t/t/t4t5t6t6t6$t6&t6yt6zt6t6t6t6t6t7t7't7*t7@t7Kt7ot7pt7st7tt7t7t7t7t7t8t8 tt8,t8Gt8Kt8Ut8ft8}t8t8ttt)tOtttttt`ZThe bacteriophage P22 arc and mnt repressors. Overproduction, purification, and properCellularnnn Wn n n Un n nXnnnnZn8nnDnn nn{nnnnnnnnn nnnnn 3n!7n!an"n"n%n&0n&zn*n0nn0nannPnSnTn n OnS)SSwssssssAnfinsenggggggggggggggggg g$g#g"g!g'g&g%g5ggggxgzg g g g g g 4g 5g 6g g Tg gg,g+gggggggggggggg=g<g;g>g/    9 2003 May|uThe Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to  2382f`Fronticelli, C. Brinigar, W.S. Olson, J.S. Bucci, E. Gryczynski, Z. Odonnell, J.K. Kowalczyk, J. 1993DIRECTED MUTAGENESIS DISTAL HISTIDINE ESCHERICHIA-COLI GLOBIN LIGAND-BINDING OXYGEN BINDING PROTEINS SEQUENCE-SPECIFIC PROTEOLYSIS SPERM WHALE MYOGLOBIN TETRAMERSUsing the mutagenesis and a gene expression system previously described [Fronticelli et al. (1991) J. Protein Chem. 10, 495-501], we have replaced Val67E11 in the distal heme pocket of the beta-chains of hemoglobin with Thr. The valine to threonine substitution is isosteric and only modifies the polarity of the beta-heme environment. The absorption and CD spectra of the resultant mutant hemoglobin were essentially the same as that of wild-type protein, indicating that the mutation did not cause any large conformational changes and that a water molecule was not coordinated to the ferrous iron atom. Equilibrium measurements of oxygen binding to the mutant indicate a 2-fold decrease in overall affinity relative to native or wild-type human hemoglobin. Thermodynamic analyses of O2 binding curves, based either on the sequential Adair model or on the MWC two-state model, indicated that the overall decrease of O2 affinity in the system was due to a lower association equilibrium constant for the intermediates of oxygenation, particularly those involved at the third ligation step. The functional characteristics of the mutant hemoglobin in either the T- or R-state were not modified greatly by the mutation; however, the Bohr effect and sensitivity to Cl- were increased, suggesting a role of the intermediates of oxygenation in the modulation of these parameters. Kinetic measurements of the last step (Hb4X3 + X --> Hb4X4) in ligand binding showed that the betaVal67(E11) --> Thr mutation decreases the O2 association rate constant roughly 2-fold, has no effect on the O2 dissociation constant, has no effect on the CO association rate constant, and increases the CO dissociation rate constant roughly 2-fold. The net result of these effects is a 2-fold decrease in the equilibrium constant for both O2 and CO binding to beta subunits in the triliganded intermediate. Unexpectedly, the betaVal67(E11) --> Thr mutation caused a 3-fold increase in the rate of CO binding to beta-subunits within T-state deoxyhemoglobin.e~Recombinant Human Hemoglobin - Modification of the Polarity of the beta-Heme Pocket by a Valine(67)(E11) -> Threonine Mutation Biochemistry325f 1235-1242m 9 Feb 2383XQFrydman, J. Nimmesgern, E. Erdjumentbromage, H. Wall, J.S. Tempst, P. Hartl, F.U.n 1992BINDING-PROTEIN CLONING ESCHERICHIA-COLI FIREFLY LUCIFERASE GROE MITOCHONDRIAL MOLECULAR CHAPERONES POLYPEPTIDE-1 PROTEIN FOLDING RIBULOSE BISPHOSPHATE CARBOXYLASE SEQUENCE-ANALYSIS T-COMPLEX POLYPEPTIDE T-HAPLOTYPES TUBULINvpFunction in Protein Folding of TRiC, a Cytosolic Ring Complex Containing TCP-1 and Structurally Related Subunits EMBO Journal1113 4767-4778 Dect 238482Frydman, J. Nimmesgern, E. Ohtsuka, K. Hartl, F.U. 1994& CHAPERONES HSP70 DNAJ HSP40 TRIChaFolding of Nascent Polypeptide Chains in a High Molecular Mass Assembly with Molecular ChaperonesR Nature 370 111-117 Frydman, J. Hhfeld, J.  199760Chaperones get in touch: the Hip-Hop connection$Trends in Biochemical Sciences223 87-92 JLFz+~|5$Lockless, S.W. Ranganathan, R. 1999VOEvolutionarily conserved pathways of energetic connectivity in protein familiesScience 286295-299tnLodi, P.J. Garrett, D.S. Kuszewski, J. Tsang, M.L. Weatherbee, J.A. Leonard, W.J. Gronenborn, A.M. Clore, G.M. 1994b\High-resolution solution structure of the beta chemokine hMIP-1 beta by multidimensional NMRSciencer  UNITED STATESe 263i 5154 1762-7Scienceo 0036-8075 94182137NHAmino Acid Sequence Computer Graphics Cytokines Human Hydrogen Bonding Hydrogen-Ion Concentration Interleukin-8 Models, Molecular Molecular Sequence Data Molecular Weight Monokines Nuclear Magnetic Resonance Protein Conformation Protein Structure, Secondary Sequence Alignment Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. The three-dimensional structure of a member of the beta subfamily of chemokines, human macrophage inflammatory protein-1 beta (hMIP-1 beta), has been determined with the use of solution multidimensional heteronuclear magnetic resonance spectroscopy. Human MIP-1 beta is a symmetric homodimer with a relative molecular mass of approximately 16 kilodaltons. The structure of the hMIP-1 beta monomer is similar to that of the related alpha chemokine interleukin-8 (IL-8). However, the quaternary structures of the two proteins are entirely distinct, and the dimer interface is formed by a completely different set of residues. Whereas the IL-8 dimer is globular, the hMIP-1 beta dimer is elongated and cylindrical. This provides a rational explanation for the absence of cross-binding and reactivity between the alpha and beta chemokine subfamilies. Calculation of the solvation free energies of dimerization suggests that the formation and stabilization of the two different types of dimers arise from the burial of hydrophobic residues.nJLF Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892..(http://biomednet.com/db/medline/94182137 4609Lodish, H.F. Kong, N. 1991CIS-TRANS ISOMERASE COMPLEMENTARY-DNA CYCLOPHILIN CYTOSOLIC BINDING-PROTEIN FK506-BINDING PROTEIN GOLGI-COMPLEX HEPATOMA SECRETORY PROTEINS IMMUNOSUPPRESSANT FK506 MATURATION PEPTIDYL-PROLYL ISOMERASEhaCyclosporin-A Inhibits an Initial Step in Folding of Transferrin Within the Endoplasmic Reticulum&Journal of Biological Chemistry 26623 14835-14838  15 Aug 4610Lodish, H.F. Kong, N. 1993ASIALOGLYCOPROTEIN RECEPTOR BINDING-PROTEIN BPTI FOLDING PATHWAY GONADOTROPIN BETA SUBUNIT HUMAN HEPATOMA-CELLS ISOMERASE KINETICS PANCREATIC TRYPSIN-INHIBITOR RIBONUCLEASE-AThe Secretory Pathway Is Normal in Dithiothreitol-Treated Cells, But Disulfide-Bonded Proteins Are Reduced and Reversibly Retained in the Endoplasmic Reticulumo&Journal of Biological Chemistry. 268-27 20598-20605 25 Sep 4611.'Lodmell, J.S. Tapprich, W.E. Hill, W.E. 1993{DEACYLATED TRANSFER-RNA ELONGATION CYCLE IDENTIFICATION MODEL PEPTIDYLTRANSFERASE CENTER STEADY-STATE SUBUNIT TRANSLOCATIONvpEvidence for a Conformational Change in the Exit Site of the Escherichia-Coli Ribosome upon Transfer RNA Binding Biochemistry3215 4067-4072i 20 Apr# Structure# s$  s*J s$ s$4 s$5 s$6 s$7 s$; s$: s$H s$I s$T s$] s$\ s$` s$a s$p s$t s$} s$~ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s$ s*E s%  s% s% s% s% s%; s* s%< s%A s%B s%B s%B s%B s%B s%B s%B s%B s%B s%B s%B s%B sNCE SITE~Transformation of the Signal Peptide/Membrane Anchor Domain of a Type-II Transmembrane Protein into a Cleavable Signal Peptide&Journal of Biological Chemistry 268 4 2699-2704 5 FebNGRoy, S. Ratnaswamy, G. Boice, J.A. Fairman, R. McLendon, G. Hecht, M.H.` 1997rkA protein designed by binary patterning of polar and non-polar amino acids displays native like properties..(Journal of the American Chemical Society 119@ 5302-5306d SJ,withg7DCDdD)D)D&DDDDD D ND ZD [D \D _D D D D D!D!D!'D!DD!fD!oD!D)D!D!D!D!D"D"4D"ED"MD"uD"xD"wD"yD"D"D)D# D#/D#0D#^D#qD#zD#{D#D#D#D#D#D#D#D#D#D#D#D#D'J33algnSnZnge,3333 3373333 Y3 \3 _3 3 3!3!'3!D3!f3!o3!3!3),3"E3"M3"w3"y3"3"3)3# 3#3#L3#^3#q3#z3#{3#3#3)63$U3$3$3%&3%'3%3'P3%33algnSnZnge,nge!%Statese!/I!CI!XI!YI!I)I!I!I!I!I"I"I"!I"_I"I"I"I"I"I#I#I#I#I#.I#EI#fI#I#I$I$I$%I$)I$*I$>I$ZI$bI$fI$I$I$I$I$I$I) I$I$I$I%I%(I%,I&I%tI*I%I%I%I%I%I%I%I%I%IS. Gov't, P.H.S. Translation, Geneticr<6As proteins are integrated into the membrane of the endoplasmic reticulum, some hydrophilic polypeptide segments are transported through the translocation channel, others remain in the cytosol, and hydrophobic transmembrane sequences are released into the lipid phase. We have addressed the molecular mechanism by which these events occur. We demonstrate that both the lumenal and the cytosolic domains of a membrane protein are synthesized while the ribosome is mem' Framework  n n# nH n n#< n * s_ s'J s58 s6  s6 s61 s6m s6r s7o s8a s8{ s8 s. sX n ncart e!kk_k t$rt)t+fs2r's3 's3's3's4b's4l's4's5U's6's6's73's7's8's8p's8x's%schit8 t tic h h himontg4X'isc7'c)$co& g+d o)F o1{' o2z' o2' o2' o2' o4A' o4' o6' k6' k6' k6!' k61' k6v' k6' k6' k6' k77' k78' k79' k7' k7' k7' k6' k8+' k8' k8' k4'k2o%isq4jq#cq gione  i T i iJ i!C i% i% i i*6k e e)e Ve5eeeLeee~e.ee0e5^e7_e7e e6ee l 2?`!!x!0!!3(6!P 77744-Taylor, J.W. Shih, I.L. Lees, A.M. Lees, R.S.t 1993AMPHIPHILIC PEPTIDES APOLIPOPROTEINS ATHEROSCLEROSIS BETA-STRAND BINDING DOMAIN CIRCULAR-DICHROISM CONFORMATION DENSITY LIPOPROTEIN RECEPTOR DESIGN HELIX-FORMING TENDENCIES LIPOPROTEINS OCCURRING AMINO-ACIDS RABBIT ARTERIAL-WALL SECONDARY STRUCTURE STABILITY SURFACE BINDINGSurface-Induced Conformational Switching in Amphiphilic Peptide Segments of Apolipoprotein-B and Apolipoprotein-E and Model Peptides<5International Journal of Peptide and Protein Researcht416L536-547 Jun 0010527739 141.1. 1999 NovnhAnalysis of dipolar-coupling-mediated coherence transfer in a homonuclear two spin-12 solid-state system 18-28FHomonuclear dipolar-mediated coherence transfer (DCT), a through-space transfer of magnetization between like spins, can yield otherwise difficult-to-obtain structural information for macromolecules by measuring the internuclear distances between two sites of interest. The behavior of a spin-12 system under DCT is analyzed in detail by computing the time development of the density matrix using the product operator formalism. The effect of coherence transfer (CT) via the homonuclear isotropic scalar coupling on DCT is examined. Analytical and computational results that yield useful information on the frequencies, first-maxima, and first-zero of CT for a uniaxially oriented or a single-crystal solid-state system are presented. The results predict that the evolution of the spin angular momentum operators under the homonuclear dipolar coupling Hamiltonian leads to "cylindrical mixing" unlike "isotropic mixing" due to the strong scalar coupling Hamiltonian. These results will find relevance in both the design of RF pulse sequences for the structural studies of uniaxially oriented biological solids and the interpretation of solution NMR results from proteins embedded in partially oriented bicelles. Copyright 1999 Academic Press.'f_Biophysics Research Division, The University of Michigan, Ann Arbor, Michigan, 48109-1055, USA.$Taylor, D. M. Ramamoorthy, A."0 1090-7807 Journal article J Magn Resonnghttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=0010527739 Taylor, W. R. 20020)A 'periodic table' for protein structures8 Nature 416u 6881657-60.e11948354 JAH1ZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11948354 7778VOTazawa, S. Unuma, M. Tondokoro, N. Asano, Y. Ohsumi, T. Ichimura, T. Sugano, H.B 1991BOUND RIBOSOMES CROSS-LINKING ENDOPLASMIC-RETICULUM MEMBRANES INVITRO NASCENT PREPROLACTIN RAT-LIVER RIBOPHORINS SECRETORY PROTEIN SIGNAL RECOGNITION PARTICLE TRANSLOCATIONjcIdentification of a Membrane Protein Responsible for Ribosome Binding in Rough Microsomal MembranesDJournal of Biochemistry 1091 89-98 Jan 7779B;Tbarka, N. Richardmereau, C. Formstecher, P. Dautrevaux, M.t 199390-KDA ANTIBODIES CDNA DNA-BINDING GLUCOCORTICOID RECEPTOR HEAT SHOCK PROTEIN, 90 KDA HEAT-SHOCK PROTEIN HSP90 NUCLEOTIDE-SEQUENCE PROGESTERONE-RECEPTOR REGION STEROID-BINDING DOMAINBiochemical and Immunological Evidence That an Acidic Domain of hsp-90 Is Involved in the Stabilization of Untransformed Glucocorticoid Receptor Complexes FEBS Letters 3222125-128 10 MayPITcherkasskaya, O. Knutson, J.R. Bowley, S.A. Frank, M.K. Gronenborn, A.M.\ 2000leNanosecond dynamics of the single tryptophan reveals multi-state equilibrium unfolding of protein GB1 Biochemistry39 11216-11226 JAH  Teeter, M.M. 199182Water-Protein Interactions - Theory and Experiment<5Annual Review of Biophysics and Biophysical Chemistry20577-600 7780INCOMPLETE COMPUTER-SIMULATION CONFORMATIONAL DIFFERENCES CRYSTAL-STRUCTURE ELECTROSTATIC POTENTIALS LIQUID WATER MOLECULAR-DYNAMICS PANCREATIC TRYPSIN-INHIBITOR PARTIAL ATOMIC CHARGES POTENTIAL FUNCTIONS X-RAY 7781& Teeter, M.M. Roe, S.M. 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Uitto, J.  1993ABNORMALITIES BLISTERING SKIN DISEASES COILED-COIL CUTANEOUS BASEMENT MEMBRANE ZONE DISEASES EPIDERMOLYSIS BULLOSA EXPRESSION FILAMENTS HETERODIMER K5 KERATIN MUTATIONS LINKAGE SEQUENCE Identification of a Leucine-to-Proline Mutation in the Keratin-5 Gene in a Family with the Generalized Kobner Type of Epidermolysis Bullosa SimplexyHuman Mutation22e 94-1026/Dong, D. Ruuska, S. E. Levinthal, D. J. Noy, N.4 1999rlDistinct roles for cellular retinoic acid-binding proteins I and II in regulating signaling by retinoic acid J Biol Chem5 2743423695-8.10446126 JAHhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=10446126 http://www.jbc.org/cgi/content/full/274/34/23695 http://www.jbc.org/cgi/content/abstract/274/34/23695Dong, F. Zhou, H. X. 2002tmElectrostatic contributions to T4 lysozyme stability: solvent-exposed charges versus semi-buried salt bridges Biophys J8331341-7.12202359 JAH@ZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=12202359'VODepartment of Physics, Drexel University, Philadelphia, Pennsylvania 19104 USA.d2+Doniach, S. Bascle, J. Garel, T. Orland, H.P 1995PJPartially folded states of proteins: characterization by X-ray scattering. 254960-967"Journal of Molecular Biology SJEi 17966/Doniger, J. Landsman, D. Gonda, M.A. Wistow, G.  1992COMPLEX CRYSTAL-STRUCTURE ESCHERICHIA-COLI FILAMENTOUS BACTERIOPHAGE IKE MOLECULAR-CLONING NUCLEAR MAGNETIC-RESONANCE PROTEIN SECONDARY STRUCTURE SEQUENCE Y-BOXThe Product of unr, the Highly Conserved Gene Upstream of N-ras, Contains Multiple Repeats Similar to the Cold-Shock Domain (CSD), a Putative DNA-Binding Motifu New BiologistP44389-395e Apr 1797*$Donlan, M.L. Brown, F.K. Jeffs, P.W. 1992AQUEOUS-SOLUTION BIG ENDOTHELIN STRUCTURE BIOLOGICAL-ACTIVITY CELLS CONVERTING ENZYME DISTANCE GEOMETRY CALCULATIONS H 1 NMR METALLOPROTEINASE INHIBITOR NMR-SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE PEPTIDE SOLUTION STRUCTURE BY NMR6/Solution Conformation of Human Big Endothelin-1s"Journal of Biomolecular NMR 2n5407-420 Sep 1804,&Donn:er, J. Caruthers, M.H. Gill, S.J. 1982jdBUFFERS. CALORIMETRY. ESCHERICHIA COLI/GE [GENETICS]. HYDROGEN-ION #CONCENTRATION. ISOPROPYL THIOGALACTOSIDE/PD [PHARMACOLOGY]. ISOPROPYL #P.H.S. THIOGLYCOSIDES/PD [PHARMACOLOGY]. THIOGLYCOSIDES #THIOGALACTOSIDE. KINETICS. PLASMIDS. REPRESSOR PROTEINS #TRANSCRIPTION FACTORS/ME [METABOLISM] [METABOLISM]. SUPPORT, U.S. GOV'T, NON-P.H.S. SUPPORT, U.S. GOV'TXQA calorimetric investigation of the interaction of the lac repressor with induceri&Journal of Biological Chemistry 25724 14826-14829 25 Dec!k DIchroism!z s! s! s! s"R s"S s"h s" s" s# s# s#[ s#\ s#` s# s# s# s# s# s# s# s$ s$+ s$: s$t s$| s$ s%  s%) s%H s%N s%b s%} s% s% s% s% s% s% s% s& s&& s&( s&1 s&H s&_ s&b s&h s& s& s& s)( s sr sr s'O s!u s+o s+q s+x s  s] s'OThatE+ge+he+ie+je+le&ee)Deee+oe+qe'Peoe)2e+re'Qe+xe+ye+{e+}e+~e+e+e+eOeee#Le,e-e,eNe'Sese+e+te+Ye+se#y0y0y0y0y0y0y0y0y0y0y0y0y0y0y0y0y0y0y1y#y#yy5Fcgih5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H5H6H6H6H6H6H6H6H6H6H6 H6 H6 H6 H6 H-wI-----. .3-.S.T.c.g-,/.. s.////M/_/u.,b../-P//////-000 030?0T0M)0w000000011#1'0J, FibriNogen o o o o4 o& o o o O  O O O O O O  O> O~ OO Os L L L L L L L L L L L L4 L L L L%] L& L L. LLYSIS ticW OO'blast s s s s Q s sT sq sd s$ s&7 s& s/ s6) s s s s  sZ s s$ s/ s6) s6) sD s   l  o0K 0V 0N   O> O~ OO Os L L L L L L L L L L L L4 L L L LLYSIS ticW OO'blast s s s s Q s sT sq sd s s s s  sZ s sD s   l  o   resonance S Ss S S S S SE S S S S Sq S S Sf S S S S S S S S S S  S > S M S  S  S  S!{ S! S! S" S"G S" S" S# S) S# S$ S$4 S$U S$\ S$ S% S% S%$ S%N S%b S% S'W S% S% S% S% S% S% S% S% S% SͻwwwwwfwfwffffUfUfUUUUDUDUDDDD4DDDDDDUDUDUDUUUUUUfUfUfUffffwfwfwwwwwwͪffUfUUDD44""""""""""""""""""""""""""""44DDDDUUffwwwwf178222 2 2&2F222f222w222 2 2!T2!p2&(2=2/2021:24222 2111"71"0$0/0406060001^22483d3394e4"V4&5f55!'9`6b6d748g8,8h9 91x9i9%9^666-66 6 6 76 6]6]6]6 [7 [=v c4t i w nu yn| y} yx zy |G  z  /~  ! b  |' _ _ _ ___ y y ya zJ` zc zy $CoLiV$L$L$L$L$L$L$L%L% L%L%L%L%L%L%!L%/L%eL%vL%L%L%L%L%L%L%L%L%L%L%L&L&L& L& L&L&)L&-L&/L&5L&NL&VL&cL&L&L&L&{L&~L&L&L&L'L'L'!L'"L),L)1L)*L+[L+\LrLLLLS BACTERIAL PHOSPHOTRANSFERASE SYSTEM HISTIDINE-CONTAINING PROTEIN NUCLEAR MAGNETIC-RESONANCE PHOSPHOCARRIER PROTEIN SALMONELLA-TYPHIMURIUM STAPHYLOCOCCUS-AUREUS SUGAR-TRANSPORT TERTIARY STRUCTURE TWO-DIMENSIONAL NMR : 4The 18.1-kDa protein III(Glc) from Escherichia coli acts as both a phosphocarrier protein in the phosphoenolpyruvate:glycose phosphotransferase system (PTS) and as a signal-transducing protein with respect to the uptake of non-PTS sugars. Phosphorylation of III(Glc) at the N(epsilon) (N3) #CS#Ra#qa#a$a$a)a$a%!a%ra%sa%ta%a%a%a%a%a&a&a&wa)a'a)%a)4a)(a)+a),a)-a)1a))a)*a+Xa+Za+\aara+_a+`a+aa+ba+daa+ea+fa'Ja+ga+ha+ia+ja+la&aIaaa)Daa%7aa)a+oa+pa+qa'Paoa.ml.yl.zl.l.l.l.l.l.Il.l/ llll/jl/ql/hlEll(l%>l']l)l(ll/lllllllllCll.lll<llHlll(llllllllllClnll.llll<llHll&$&*tj 5098D>Michalek, M.T. Grant, E.P. Gramm, C. Goldberg, A.L. Rock, K.L. 1993jcACTIVATING ENZYME CELLS DEGRADATION E1 EXPRESSION GENE ICAM-1 MOLECULES PROTEIN TOXIC LYMPHOCYTES-TleA Role for the Ubiquitin-Dependent Proteolytic Pathway in MHC Class I-Restricted Antigen Presentation Nature 363 6429552-554 10 Jun 5099,&Michalovitz, D. Amsterdam, A. Oren, M. 1989b[Interactions between SV40 and cellular oncogenes in the transformation of primary rat cellsE 144i 63-75 4-Current Topics in Microbiology and Immunology 5100*#Michalovitz, D. Halevy, O. Oren, M. 1990rkConditional inhibition of transformation and of cell proliferation by a temperature-sensitive mutant of p53l Cell624671-680g 24 Aug 5101*#Michalovitz, D. Halevy, O. Oren, M. 1991&p53 mutations: gains or losses?i& Journal of Cellular Biochemistry451l 22-29 Jan 5102"Michiels, T. Cornelis, G.R.  1991CALCIUM CLONING ENTEROCOLITICA ESCHERICHIA-COLI HEMOLYSIN GRAM-NEGATIVE BACTERIA NUCLEOTIDE-SEQUENCE OUTER-MEMBRANE PROTEINS PSEUDOTUBERCULOSIS SIGNAL PEPTIDE VIRULENCED>Secretion of Hybrid Proteins by the Yersinia Yop Export SystemJournal of Bacteriologyt 1735 1677-1685 Mar$Michnick, S.W. Shakhnovich, E. 1998f_A strategy for detecting the conservation of folding-nucleus residues in protein superfamilies.Folding and Design3d239-251SJE JAH  5103RKMiddaugh, C.R. Steadman, B.L. Schurtenberger, P. Lee, D.C. Chlebowski, J.F.  1993ALPHA 2 MACROGLOBULIN BINDING CALORIMETRY COMPLEXES CONFORMATIONAL CHANGE CONFORMATIONAL-CHANGES DSC FAST FORMS LIGHT-SCATTERING METHYLAMINE MICROSCOPY PLASMIN PROTEINASES PURIFICATION TRYPSIN X RAY SCATTERINGChanges in Structure of alpha2-Macroglobulin upon Reaction with Trypsin as Assessed by Light Scattering and Differential Scanning Calorimetry$Biochimica et Biophysica Acta  1161 2-3328-332 13 Feb 5104Middaugh, C.R. Thomson, J.A. Burke, C.J. Mach, H. Naylor, A.M. Bogusky, M.J. Ryan, J.A. Pitzenberger, S.M. Ji, H.L. Cordingley, J.S. 1993ABSORPTION-BANDS AMINO-ACIDS BETA-TURNS CIRCULAR-DICHROISM CONFORMATION F4-6 PEPTIDE POLYPEPTIDES QUANTITATIVE IR SPECTROPHOTOMETRY SALT-BRIDGES SCHISTOSOMA-MANSONI SCHISTOSOME EGGSHELL PROTEIN STABILIZATION WATER H2O SOLUTIONS\VStructure of Synthetic Peptide Analogues of an Eggshell Protein of Schistosoma-mansoniProtein Science`2i6@900-914 Jun 5105$Middleton, R.B. 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Anfinsen, C.B.O 1963RLThe genetic control of tertiary protein structure: Studies with model system:3Cold Spring Harbor Symposia On Quantitative Biology. 128439-449 2024>7Epstein, H.F. Schechter, A.N. Chen, R.F. Anfinsen, C.B. 1971`YFolding of staphylococcal nuclease: kinetic studies of two processes in acid renaturationo603499-508 28 Sep"Journal of Molecular Biology 2025.'Erard, M. Lakhdarghazal, F. Amalric, F. 1990AMINO-ACID SEQUENCE CIRCULAR-DICHROISM GENES HISTONE H-1 NUCLEOLIN PHYSARUM-POLYCEPHALUM PROTEIN CONFORMATION SECONDARY STRUCTURE TERMINAL DOMAIN TRANSCRIPTIONALLY ACTIVE CHROMATIN`YRepeat Peptide Motifs Which Contain Beta-Turns and Modulate DNA Condensation in Chromatin& European Journal of Biochemistry 191y1 19-26 20 Jul12555083102/ 2003 Feb06/A folding machine for many but a master of nonec 84-6(!Erbse, A. Dougan, D. A. Bukau, B..22442707 1072-8368 NewsoNat Struct BioliAdenosine Triphosphate/metabolism GroEL Protein/genetics/*metabolism GroES Protein/genetics/*metabolism Luminescent Proteins/chemistry/metabolism Models, Biological Protein Folding Variation (Genetics)0lehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12555083r 2026,&Erchegyi, J. Kastin, A.J. Zadina, J.E. 1992ANTIOPIATE BARRIER BINDING-SITES CARRIER-MEDIATED TRANSPORT FOOTSHOCK-INDUCED ANALGESIA HEMORPHINS HUMAN-BRAIN MIF-1 MORPHINE OPIATE PEPTIDE RAT-BRAIN STRESS TYR MIF 1 TYR W MIF 1 TYR-MIF-1 TYR-PRO-LEU-GLY-NH2tIsolation of a Novel Tetrapeptide with Opiate and Antiopiate Activity from Human Brain Cortex - Tyr-Pro-Trp-Gly-NH2 (Tyr-W-MIF-1) Peptides134623-631Jul-Aug 2027ZSErdmann, R. Wiebel, F.F. Flessau, A. Rytka, J. Beyer, A. Frohlich, K.U. Kunau, W.H. 1991BETA-OXIDATION ENDOPLASMIC-RETICULUM ESCHERICHIA-COLI LACZ FUSIONS MEMBRANE PROTEIN TRANSLOCATION SACCHAROMYCES-CEREVISIAE GENE SENSITIVE METHOD SEQUENCE TRANSFORMATIONtmPAS1, a Yeast Gene Required for Peroxisome Biogenesis, Encodes a Member of a Novel Family of Putative ATPasesy Cell643499-510 8 Feb"Erickson, H.P. Obrien, E.T.d 199282Microtubule Dynamic Instability and GTP Hydrolysis<6Annual Review of Biophysics and Biomolecular Structure TNAnnual Reviews Inc, 4139 El Camino Way, PO Box 10139, Palo Alto, CA 94303-089721145-166  2029 CYTOSKELETON EXCHANGEABLE NUCLEOTIDE SITE FLUORIDE COMPLEXES GTP CAP GUANINE NUCLEOTIDES GUANOSINE 5'-TRIPHOSPHATE HYDROLYSIS INDIVIDUAL MICROTUBULES LATERAL CAP MODEL LIGHT-MICROSCOPY MITOTIC SPINDLE PHOSPHATE ANALOGS POLYMERIZATION TUBULIN TUBULIN-COLCHICINE COMPLEX 2028$Erickson, A.C. Johnson, G.V.W. 1993ALKALINE-PHOSPHATASE ALZHEIMERS-DISEASE CAMP-DEPENDENT PROTEIN KINASE CHELATE CHELATING SEPHAROSE IMINODIACETIC ACID PAIRED HELICAL FILAMENTS PHOSPHORYLATION PROTEINS TAU\UMetal (Fe3+) Affinity Chromatography - Differential Adsorption of Tau Phosphoproteinse&Journal of Neuroscience MethodsE463y245-249  Mar 2030D=Erie, D.A. Suri, A.K. Breslauer, K.J. Jones, R.A. Olson, W.K.C 19933-DIMENSIONAL STRUCTURE B-DNA DUPLEX FORMATION DYNAMICS ELECTROSTATIC INTERACTIONS NMR NUCLEAR MAGNETIC-RESONANCE POLYNUCLEOTIDE CHAINS PROTEINS TRANSITIONSxrTheoretical Predictions of DNA Hairpin Loop Conformations - Correlations with Thermodynamic and Spectroscopic Data Biochemistry322436-454 19 Jan 2031Erijman, L. Weber, G. 1991F?CONFORMATIONAL DRIFT DISSOCIATION DYNAMICS HYDROSTATIC-PRESSUREb`YOligomeric Protein Associations - Transition from Stochastic to Deterministic Equilibrium- Biochemistry306 1595-1599 12 Feb 2032Erijman, L. Weber, G. 1993>8CONFORMATIONAL DRIFT HIGH-PRESSURE LACTATE-DEHYDROGENASEd^Use of Sensitized Fluorescence for the Study of the Exchange of Subunits in Protein Aggregates&Photochemistry and Photobiologyy573 411-415D Mar 2039:3Eriksson, A.E. Kylsten, P.M. Jones, T.A. Liljas, A. 1988Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN- ion to the zinc at high pHt44m283-2930*Proteins: Structure, Function and Genetics 2038,%Eriksson, A.E. Jones, T.A. Liljas, A. 1988JDRefined structure of human carbonic anhydrase II at 2.0 A resolution44i274-282p0*Proteins: Structure, Function and Genetics 2037>8Eriksson, A.E. Cousens, L.S. Weaver, L.H. Matthews, B.W. 1991JCThree-dimensional structure of human basic fibroblast growth factorA888 3441-3445 15 AprVOProceedings of the National Academy of Sciences of the United States of America &Zuniga42o1Sotinr&Kr rcherneely w&doe)(s0s5[i1<'ich1L's1d's1's1's2's4@'s4's4's5j's5's5's5's5's5's6's6A's6|'s6's7's7's8u's8's8's&smant,tshia1mvia1qy1y4\y&yagaw8Swahlenk'nzigneerink*'icklzebz|t}t't't't't't)+t)*t' t.gt/'t.t0t2t3Zt45t7ftGtterion icyK y y/ydowskygg#g'!g'"g+g gmuntliczMMambmcmfmmmmm&m'#m'$m'%m/Im2m2m6m2'm*Fmogen lG,*,o/oboo}$'&smilich7Z7-..*o}$GEN.|1997/~8(8']8(8(8+8/8/808(80080\80_8)08"88)[8):8)?8)Q8'N81)8108 8)M808*;81818/818282)82R82T82S828/ 8/!82828282828283 83o838*8)8)8)848(8)8(8)848(8(848487 Chemistry7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k8 k8 k8 k8 k8 k8 k8  k8  k8 k6 k8$ k8, k8- k8/ k81 k82 k83 k84 k89 k8: k8; k8< k8? k8A k8B k8C k8E k8G k8H k8I k8J k8K k8M k8N k8P k8Q k8R k8S k8U k8X k8Y k8Y k8Y k??????720037373737373737373738383838383838383838!38*38+38,38-38.38/38038138238338438638738838938:38;38<38=38>38?38@38A38B38C38D38E38F38G38H38I38J38K38L38M38N38O38P38Q38T38U38X38X3 Non-U.S. Gov't Support, U.S. Gov't, P.H.S. lehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10966114tZheng, N. Schulman, B. A. Song, L. Miller, J. J. Jeffrey, P. D. Wang, P. Chu, C. Koepp, D. M. Elledge, S. J. Pagano, M. Conaway, R. C. Conaway, J. W. Harper, J. W. Pavletich, N. P. 2002FStructure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex %  )  Nature 4166DK6Ga6Ia6Ka6Oa6Ta6Ua6Xa6Ya6Za6[a6\a6]a6^a6ea6ja6ka6ya6{a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a7a7a7a7a7a7)a7-a7/a70a71a72a7Qa7da7fa7qa7sa7xa7{a7|a7~a7a7a7a7a7a7a7a7a^^^KKKKKK^^^ FEBS Letters 287 1-2 67-70. 5 Aug7 24750*Garciaquintana, D. Garriga, P. Manyosa, J. 1993ALPHA-HELICES BACTERIORHODOPSIN CIRCULAR-DICHROISM GLOBULAR-PROTEINS IR SPECTROSCOPY POLYPEPTIDES PROTEIN SECONDARY STRUCTURES PURPLE MEMBRANE SPECTRA WATERQuantitative Characterization of the Structure of Rhodopsin in Disc Membrane by Means of Fourier Transform Infrared Spectroscopy&Journal of Biological Chemistry 2684 2403-2409 5 Feb j 8ynthesis of leader peptidase is repressed, protein precursors accumulate, including the precursors of phage M13 coat protein (an inner membrane protein), maltose-binding protein (a periplasmic protein), and OmpA protein (an outer membrane protein). These precursors are translocated across the plasma membrane, as judged by their sensitivity to added proteinase K. However, pro-OmpA and pre-maltose binding protein are retained at the outer surface of the inner membrane. Thus, leader peptides anchor translocated pre-proteins to the outer surface of the plasma membrane and must be removed to allow their subsequent release into the periplasm or transit to the outer membrane. 0021-9258zLeader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane&Journal of Biological Chemistry 26029 15925-15931 ° P 1530 °&Dahlstrom, A.B. Czernik, A.J. Li, J.Y. 1992hbAXONAL-TRANSPORT BOVINE BRAIN KINESIN CENTRAL NERVOUS-SYSTEM CGRP CHROMOGRANIN-A FORCE-GENERATING PROTEIN GENE-RELATED PEPTIDE KINESIN MATRIX PEPTIDES MICROTUBULE-BASED MOTILITY RETINAL GANGLION-CELLS SMALL SYNAPTIC VESICLES SV2 SYNAPSIN I LIKE SYNAPSIN-IA AND SYNAPSIN-B SYNAPSIN-II-A AND SYNAPSIN-II-B SYNAPTOPHYSIN TERMINAL-SPECIFIC PHOSPHOPROTEIN VIPOrganelles in  53280)Mossakowska, D.E. Nyberg, K. Fersht, A.R. 1989Kinetic characterization of the recombinant ribonuclease from Bacillus amyloliquefaciens (barnase) and investigation of key residues in catalysis by site-directed mutagenesis Biochemistry289a 3843-3850r 2 May 5330 Mossing, M.C. Sauer, R.T. 1990BACTERIOPHAGE-LAMBDA CONFORMATION DNA HOST STRAINS NUCLEOTIDE-SEQUENCES PHAGE CLONING VECTORS PROTEIN PUC19 VECTORS REPRESSOR STABILITY0hbStable, Monomeric Variants of Lambda-Cro Obtained by Insertion of a Designed Beta-Hairpin SequenceScience 2501 4988 1712-1715 21 Dec2KDBv2NA2MA2LA2PA2QA2RA2TA2SA2VA2XA2ZA2YA2[A2\A2]A2_A2^A2`A2aA2bA2dA2cA2eA2fA2gA2iA2hA2jA2nA2mA2oA2pA2qA2rA2sA2tA2uA2vA2wA2xA2yA2zA2{A2|A2}A2~A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2Ao Y o o o o^ o oichiometricr r rateUG UL TY T T T  T  T' T T* T T6 T) T 1 T 0 T-  RdigerS2P!.Rdiger, S. 2Pr, M. P. Schneider-Mergener, J. Bukau, B.terial 3!.nd Medline-d2Ped databases contains material from copyrighted publications and users are therefore advised that downloading for re-distribution is subject to copyright restriP83Kamal@tanir/ri,h6l8l$loebkkar(walyabbehonjohr"r{e3*ena3+ttanii/i/kubon nogawah97skiyAtaniry$tsosyaFk$kketar*jmererl2meiersheidt*lott!ogashira shita- pe huisy"?t1eingar2ttekar0n2agawayyixm"m"morin8ycin o8 o%*okayagg host... Searching for: [mori+K*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Connecting to host... Connecting to host... Searching for: [mori+K*[AUTH]+AND+Cell[JOUR]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retr2nFOrme2ma2oa2pa2qa2ra2sa2ta2ua2va2wa2xa2ya2za2{a2|a2}a2~a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a1ja1Va2a2a2a1989 Prager1989 Prakash1993 Prakash1993 YPramanik1992-CPramanik1998 Pranata1991IPrantera19922 Prasad1990 " Prasad1991  Prasad1991  Prasad1992  Prasad1992  Prasad1993  Prasad1993  Prasad1993 z Prasher1993(Prat Gay1997 Pratesi1991 Pratesi1993 Pratje199194 Pratje19911 Pratsch1991| Pratt1990  Pratt1990 Pratt1990twoy(y:y(y[yyyyyyyy "y oy py zy y!y!Iy!y!y!y!y" y"y"0y"py"vy"y)Oy*8y#,y#y#y#y$Zy%'y%Ry%y%y%y%y%y&y&.y&1y&gy&y&y+]y+y+dyy+y+y+y*y!wy+y+By+y&y&y ﯪ  ( ! ;믪*%" @ $   ﮪ*  @ !퀈( ﯿ +  `! t   6587$Robertson, A.D. Baldwin, R.L.s 1991ACID ALPHA-LACTALBUMIN AMIDE PROTON-EXCHANGE COOPERATIVE TRANSITIONS MOLTEN-GLOBULE STATE NMR NUCLEAR MAGNETIC-RESONANCE PANCREATIC TRYPSIN-INHIBITOR PROTEIN STABILITY SPECTROSCOPYHydrogen exchange has been used to test for the presence of nonrandom structure in thermally denatured ribonuclease A (RNase A). Quenched-flow methods and 2D H-1 NMR spectroscopy were used to measure exchange rates for 36 backbone amide protons (NHs) at 65-degrees-C and at pH* (uncorrected pH measured in D2O) values ranging from 1.5 to 3.8. The results show that exchange is approximately that predicted for a disordered polypeptide [Molday, R. S., Englander, S. W., & Kallen, R. G. (1972) Biochemistry 11, 150-158]; we thus are unable to detect any stable hydrogen-bonded structure in thermally denatured RNase A. Two observations suggest, however, that the predicted rates should be viewed with some caution. First, we discovered that one of the approximations made by Molday et al. (1972), that exchange for valine NHs is similar to that for alanine NHs, had to be modified; the exchange rates for valine NHs are about 4-fold slower. Second, the pH minima for exchange tend to fall at lower pH values than predicted, by as much as 0.45 pH units. These results are in accord with those of Roder and co-workers for bovine pancreatic trypsin inhibitor [see Table I in Roder, H., Wagner, G., & Wuthrich, K. (1985) Biochemistry 24, 7407-7411]. The origin of the disagreement between predicted and observed pH minima is unknown but may be the high net positive charge on these proteins at low pH. In common with some other thermally unfolded proteins, heat-denatured ribonuclease A shows a significant circular dichroism spectrum in the far-ultraviolet region [Labhardt, A. M. (1982) J. Mol. Biol. 157, 331-355]. This spectrum is reduced to a low level by adding guanidine hydrochloride. The nature of the residual structure responsible for this spectrum is not known. Our results show that it is not stable helix formation by the three alpha-helices of native ribonuclease A, which would give measurable protection against amide proton exchange.f>7Hydrogen Exchange in Thermally Denatured Ribonuclease-A Biochemistry3041 9907-9914 15 Oct 6589 Robertson, M. 1992&Alzheimer's Disease and Amyloide Nature 356, 6365 103 12 Mar 6588Robertson, D.E. Farid, R.S. Moser, C.C. Urbauer, J.L. Mulholland, S.E. Pidikiti, R. Lear, J.D. Wand, A.J. DeGrado, W.F. Dutton, P.L. 1994PROTEIN DESIGN2+Design and Synthesis of Multi-Haem Proteins  Nature 368425-432haRobien, M.A. Clore, G.M. Omichinski, J.G. Perham, R.N. Appella, E. Sakaguchi, K. Gronenborn, A.M. 1992Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyl transferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of escherichia-colim Biochemistry3113 3463-3471 7 Apr 6590 ACETYLTRANSFERASE COMPONENT ACYLTRANSFERASE COMPONENTS BACILLUS-STEAROTHERMOPHILUS INTERPROTON DISTANCE RESTRAINTS MOLECULAR-DYNAMICS NUCLEAR MAGNETIC-RESONANCE NUCLEOTIDE-SEQUENCE POTATO CARBOXYPEPTIDASE INHIBITOR PYRUVATE-DEHYDROGENASE SACCHAROMYCES-CEREVISIAE 6591PIRobinson, B.H. Sherwood, W.G. Mayes, S. Freire, E. Oei, J. DiBattista, D.` 1980jcAGING. ANIMAL. ANIMALS, NEWBORN. BLOOD GLUCOSE/ME [METABOLISM] BRAIN/EN [ENZYMOLOGY]. BRAIN/GD [GROWTH AND DEVELOPMENT]. FETUS #GLUCOKINASE/ME [METABOLISM]. GLUCOSE/ME [METABOLISM]. HAPLORHINI HEXOKINASE/ME [METABOLISM]. LACTATES/ME [METABOLISM]. LIVER #[ENZYMOLOGY]. LIVER/GD [GROWTH AND DEVELOPMENT]. MACACA #[METABOLISM]. MACACA MULATTA/ME [METABOLISM]BjdFactors affecting glucose turnover and utilization in the neonatal subhuman primate (Macaca mulatta)Biology of the Neonate37 1-2 60-669600 06%08.0\01o01q02L02a02b020/0p0,3$(060B0002v9252v2/27476)3676469920P4R66I772489.7)29728891)D11201)/1668667&70661=1y81# 0#0'"00{0,T00070000P062066R1!%3.2+y21753+y33'T9822~)3 4707327!7293~5!%8'P80705616705)6818.9)41452!2 33+c08636+c17]51717>21752627752~366016.4)(5+r67092+r3+r3ts - Biochemistry and Molecular Biologyx4n102-105 5853 INCOMPLETE 58610*Pachter, R. Arrowsmith, C.H. Jardetzky, O. 19923-DIMENSIONAL NMR-SPECTROSCOPY C-13 H-1 NUCLEAR OVERHAUSER E+}PRotein+~+++++++ ++++ ,&F)|{"#L *,,WV#O '*yF ]!9 AnqpM pqtein cowseJournal of Dairy Science757 1891-1900 JulM 43162+Leatherbarrow, R.J. Fersht, A.R. Winter, G.S 1985pjTransition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering8223 7840-78443 Dec0VOProceedings of the National Academy of Sciences of the United States of America4 4314& Leatherbarrow, R.J. Fersht, A.R. 1986Protein engineeringlProtein EngineeringK-CFOr-KC-SC-jC-oC-uC-C}CC^C-C-C-C-C, C-C-C-C-C-C-C-C-C-C-C.C.C.C.#C.$C.)C.,C.-C CC.NC.\C.wC.C.C.C.C.C+C.C.C.C.C.C.C.C.C.C-CC.C+GC-C(C.C.C.C.C.Cd 3D models to be constructed using distance geometry. NOE back-calculation was used to check the validity of the final models. Strong variations of internal motion amplitude have been found in both peptides along their backbone. Motions with high amplitudes have been localized in the Gly-Pro-Gly sequence which forms a beta-turn in both structures.lfStructural and Dynamic Studies of 2 Antigenic Loops from Haemagglutinin - A Relaxation Matrix Approach"Journal of Biomolecular NMRe3 MEchanism l l l l l l l l+ l l l l& lt l lb lq l' l l l l< lY lZ la lR la le l lb l~ l l l lA l l l, lF l} l l l  l X l  l! l! l! l! l" l"' l" l" l#a l#i l# l% l%I l% l% l% l% leeoeeee*eaeeeyepeeJe 1e Pe e Xe e Oe bezeeeee%e|eeeeeeeeyeeeie ee e"e'eLeOeQeeeeeGe.eeeeheee 4e!e!e!e"oe1pNlm1qS1rS1sS1tS1uS1vS1wS1xS1yS1zS1{S1|S1}S1~S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S1S AssociationN x xP x xI x  x  x  x 9 x ; x  x ^ x'  xj xb x x x x xR x] xt xE x x8 x? xA x x x> xC x x5 x_ xm x x x x x x! x* x. x& x@ xo xs x x x  x!  x!N x" x" x" x" x# x# x&M x&L x& x&{ x1NCbi1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1d1dansfer RNA Synthetaseu&Journal of Biological Chemistrye 267r32 22703-22706 15 Nov 7175LFShibata, A. Yamamoto, M. Yamashita, T. Chiou, J.S. Kamaya, H. Ueda, I. 1992voALBUMIN BILAYERS COIL TRANSITION INTERFACIAL ACTION MOLECULES PHOSPHATIDYLCHOLINES POLY L LYSINE PROTEINS WATER~wBiphasic Effects of Alcohols on the Phase Transition of Poly(L-Lysine) Between alpha-Helix and beta-Sheet Conformationsr Biochemistry3125 5728-5733 30 Jun  8h /6Z  z(tCreighton, T.E. 19946/The energetic ups and downs of protein folding. Nature Structural Biology1 3135-138d JAH Creighton, T.E. 1995An unfolding storyCurrent Biology5353-356dSJE JAHCreighton, T.E. 1997F@How important is the molten globule for correct protein folding?$Trends in Biochemical Sciences22 6-10 SJE6 1464Creuzet, F. McDermott, A. Gebhard, R. Vanderhoef, K. Spijkerassink, M.B. Herzfeld, J. Lugtenburg, J. Levitt, M.H. Griffin, R.G.a 1991@9MAGIC-ANGLE POLYCRYSTALLINE SOLIDS SPECTRA SPIN DIFFUSION@b[Determination of Membrane Protein Structure by Rotational Resonance NMR - BacteriorhodopsinrScience 251i 4995783-786 15 Feb Crickmore, N. Ellar, D.J.  1992~Involvement of a Possible Chaperonin in the Efficient Expression of a Cloned CryIIA -Endotoxin Gene in Bacillus-ThuringiensisMolecular Microbiology6 11 1533-1537 Jun 1465ngELECTROPORATION ESCHERICHIA-COLI INSECTICIDAL CRYSTAL PROTEINS STRAINS SUBSP ISRAELENSIS TRANSFORMATION^XThe Bacillus thuringiensis cryllA delta-endotoxin gene is found as the third-gene in a three-gene operon, with a sporulation-dependent promoter lying upstream of the first gene, orf1. We show here that the polypeptide product of the middle gene (orf2) is required for efficient expression of the toxin gene. In the absence of a functional ORF2 polypeptide the toxin does not form the crystalline inclusions characteristic of other known Bacillus thuringiensis toxins. We discuss the importance of this finding with respect to the possible role of chaperonins in the crystallization of these proteins. 1466 Crippen, G.M. 1991^XPrediction of Protein Folding from Amino Acid Sequence over Discrete Conformation Spaces Biochemistry3017 4232-4237@ 30 Apr 1467D=Crisma, M. Valle, G. Bonora, G.M. Toniolo, C. Cavicchioni, G.  1993xqALPHA-HYDROXYISOBUTYRIC ACID DEPSIPEPTIDES AMINO-ACIDS AMINOISOBUTYRIC-ACID BETA-BEND RIBBON SPIRAL BETA-BENDS CONFORMATIONAL-ANALYSIS CRYSTAL-STATE CONFORMATION DEPSIPEPTIDE CONFORMATION DERIVATIVES INFRARED ABSORPTION L ALA OME LINEAR OLIGOPEPTIDES NUCLEAR MAGNETIC-RESONANCE PENTAPEPTIDE PREFERRED CONFORMATION SOLID-STATE TRIPEPTIDE X RAY DIFFRACTION X-PRO PEPTIDESNThe beta-Bend Ribbon Spiral - Synthesis and Conformational Analysis in Solution and in the Crystal State of Depsipeptides Containing alpha-Hydroxyisobutyric AcidP<5International Journal of Peptide and Protein ResearchA416N553-560 JunHBCristobal, S. Scotti, P. Luirink, J. von Heijne, G. de Gier, J.W.L 1999The signal recognition particle-targeting pathway does not necessarily deliver proteins to the Sec-translocase in Escherichia coli r &Journal of Biological Chemistry 27429 20068-20070 jlf 14680)Crombie, T. Swaffield, J.C. Brown, A.J.P. 1992BIOSYNTHESIS CODON BIAS DISULFIDE BONDS MULTIPLE NUCLEOTIDE-SEQUENCE PLASMID PROTEIN FOLDING SACCHAROMYCES-CEREVISIAE SELECTION TRANSFORMATION TRANSLATION TRYPTOPHAN BIOSYNTHESIS YEASTb[Protein Folding Within the Cell Is Influenced by Controlled Rates of Polypeptide ElongationT 2281I 7-12 5 NovR"Journal of Molecular Biology2113052ngBiotination of proteins in vivo. A post-translational modification to label, purify, and study proteinsPost-translational modification of proteins with biotin provides the means to specifically label proteins in vivo and to purify proteins from crude cell lysates. The carboxyl-terminal protein segments modified by reaction with biotin ligase are strongly conserved in nature. We have demonstrated that the proteins encoded by translational gene fusions of a number of heterologous proteins to these carboxyl-terminal sequences become biotinated in vivo. The minimum size of the protein segment needed to allow biotination of fusion proteins is 75 amino acids. This biotination sequence, although of bacterial origin, functions in Saccharomyces cerevisiae as well as in Escherichia coli. Fusion proteins are readily labeled with [3H]biotin in vivo and the labeling is highly specific due to the scarcity (less than 5) of biotinated protein species. Biotinated fusion proteins can be readily purified in native form by binding to columns of monomeric avidin followed by elution with buffers containing biotin. Alternatively, proteins can be purified in a denatured form in presence of 1% sodium dodecyl sulfate or 8 M urea. Thus, this technology allows purification by affinity chromatography of any protein to which a biotination sequence can be attached. The ability to specifically label a protein in vivo should have utility in studies such as intracellular protein trafficking and cytoskeletonal dynamics. 'HADepartment of Microbiology, University of Illinois, Urbana 61801. Cronan, J. E., Jr.eng Journal ArticleAmino Acid Sequence Biotin/*metabolism Comparative Study Escherichia coli/genetics Galactosidases/*genetics Molecular Sequence Data Plasmids Protein Binding *Protein Processing, Post-Translational Proteins/genetics/*isolation & purification Recombinant Fusion Proteins/isolation & purification Saccharomyces cerevisiae/genetics Sequence Homology, Nucleic Acid Support, U.S. Gov't, P.H.S. beta-Galactosidase/*genetics/isolation & purification  J Biol Chem` 1990 Jun 25 265`18 10327-33. 1469& Cronet, P. Sander, C. Vriend, G. 1993BACTERIORHODOPSIN BETA ADRENERGIC RECEPTOR BETA-2-ADRENERGIC RECEPTOR BETA-ADRENORECEPTOR CLONING IDENTIFICATION LIGAND BINDING SITE LOCALIZATION MEMBRANE PROTEIN PROTEIN STRUCTURE PREDICTION RECEPTOR RESOLUTION SEQUENCE SEQUENCE STRUCTURE ALIGNMENT0)Modeling of Transmembrane 7 Helix BundlesProtein Engineering61 59-64 Jan  9%)@.6Hl6G10731429 2973 2000 Mar 31|vFast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster791-802tnEscherichia coli cyclophilin A, a 164 residue globular protein, shows fast and slow phases of refolding kinetics from the urea-induced unfolded state at pH 7.0. Given that the slow phases are independent of the denaturant concentration and may be rate-limited by cis/trans isomerizations of prolyl peptide bonds, the fast phase represents the true folding reaction. The extrapolation of the fast-phase rate constant to 0 M urea indicates that the folding reaction of cyclophilin A is extraordinarily fast and has about 700 s(-1) of the rate constant. Interrupted refolding experiments showed that the protein molecules formed in the fast phase had already been fully folded to the native state. This finding overthrows the accepted view that the fast folding is observed only in small proteins of fewer than 100 amino acid residues. Examination of the X-ray structure of cyclophilin A has shown that this protein has only one unique hydrophobic core (phenylalanine cluster) formed by evolutionarily conserved phenylalanine residues, and suggests that this architecture of the molecule may be responsible for the fast folding behavior.'tnDepartment of Physics, School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo, 113-0033, Japan.6/Ikura, T. Hayano, T. Takahashi, N. Kuwajima, K.("20198326 0022-2836 Journal Article J Mol Biol Amino Acid Sequence Catalysis/drug effects Circular Dichroism Conserved Sequence Dose-Response Relationship, Drug Escherichia coli/*enzymology Isomerism Kinetics Models, Chemical Models, Molecular Molecular Sequence Data Molecular Weight Peptidylprolyl Isomerase/*chemistry/*metabolism Phenylalanine/chemistry/*metabolism Proline/metabolism Protein Conformation/drug effects Protein Denaturation/drug effects *Protein Folding Protein Renaturation Sequence Alignment Support, Non-U.S. Gov't Thermodynamics Urea/pharmacologylehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10731429D9433183451e 1998tnConformational studies of human islet amyloid peptide using molecular dynamics and simulated annealing methods 9-20Molecular dynamics simulations and simulated annealing in vacuum, model aqueous solution, and simulated membrane were used to analyze the conformational preferences of a segment spanning 20-29 residues of human islet amyloid polypeptide, [referred to as IAPPH (20-29)]. Molecular dynamics simulations were conducted at 300 K on IAPPH (20-29). The minimum energy conformers obtained in model aqueous solution and vacuum exhibited similar structures. Even in the absence of any constraints on peptide bonds, trans conformation was preferred consistently by all the peptide bonds. Analysis of the minimum energy conformers indicated that IAPPH (20-29) showed a strong preference for turn structures in all the environments. These turn structures were stabilized by the formation of hydrogen bonds between the backbone amide and carbonyl groups. A good agreement was found between the results obtained from the molecular dynamics simulation and solid-state nmr experimental studies.'VPBiophysics Research Division, University of Michigan, Ann Arbor 48109-1055, USA.$Ilangovan, U. Ramamoorthy, A.("98094757 0006-3525 Journal Article BiopolymersAmino Acid Sequence Amyloid/*chemistry Chemistry, Physical Computer Simulation Human Islets of Langerhans/*chemistry Molecular Sequence Data Protein Conformation Support, Non-U.S. Gov't Thermodynamicsjdhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=9433183Ill, C.R. Gonzales, J.N. Houtz, E.K. Ludwig, J.R. Melcher, E.D. Hale, J.E. Pourmand, R. Keivens, V.M. Myers, L. Beidler, K. Stuart, P. Cheng, S. Radhakrishnan, R.   1997~xDesign and construction of a hybrid immunoglobulin domain with properties of both heavy and light chain variable regionsProtein Engineering 1083949-957(82antibody, engineering, expression, gene, secretion(!Ilyina, E. Milius, R. Mayo, K. H. 1994Synthetic peptides probe folding initiation sites in platelet factor-4: Stable chain reversal found within the hydrophobic sequence LIATLKNGRKISLi    Biochemistry33 13436-13444 KSR@Im, W Brooks, CL III 2004voDe Novo Folding of membrane proteins: An exploration of the structure and NMR properties of the fd coat protein"Journal of Molecular Biology 337513-519l KSR 3429pjImamoto, N. Matsuoka, Y. Kurihara, T. Kohno, K. Miyagi, M. Sakiyama, F. Okada, Y. Tsunasawa, S. Yoneda, Y. 1992ASP GLU ASP LOCALIZATION SIGNALS MONOCLONAL-ANTIBODY PORE COMPLEX RAT-LIVER NUCLEI SIGNAL-BINDING PROTEINS STRESS PROTEINS T-ANTIGEN TRANSPORT SIGNALS UNCOATING ATPASEarkAntibodies Against 70-kD Heat Shock Cognate Protein Inhibit Mediated Nuclear Import of Karyophilic ProteinsJournal of Cell Biology 1195 1047-1061 Dec7 3430Imanishi, Y. Kimura, S. 1992PEPTIDE MEMBRANE INTERACTION PEPTIDE ORIENTATION IN MEMBRANE PEPTIDE SELF-ASSOCIATION PRIMARY AMPHIPHILICITY SECONDARY AMPHIPHILICITY SURFACE VOLTAGE-DEPENDENT ION CHANNELE<6Peptide Self-Assembly in Phospholipid Bilayer MembraneRLProceedings of the Japan Academy Series B - Physical and Biological Sciences688121-126f Octl 3431:3Imbalzano, A.N. Kwon, H. Green, M.R. Kingston, R.E. 1994PITRANSCRIPTION ON A NUCLEOSOMAL TEMPLATE FACILITATED BINDING FACTOR ACCESS D>Facilitated Binding of TATA-Binding Protein to Nucleosomal DNA Nature 370481-485n6/Imoto, T. Forster, L.S. Rupley, J.A. Tanaka, F. 1971ZTFluorescence of lysozyme: emissions from tryptophan 62 and 108 and energy migration.69 1151-1155VOProceedings of the National Academy of Sciences of the United States of America3F@Imoto, T. Johnson, L.N. North, A.C.T. Philips, D.C. Rupley, J.A. 1972Vertebrate lysozymes.  Boyer, P.D. The Enzymes New York Academic Press7(665-864 3rd/,n4~*4|*" ,)0*Prehoda, K.E. Mooberry, E.S. Markley, J.L. 1998NHPressure denaturation of proteins: evaluation of compressibility effects Biochemistry37 5785-5790@ JAH 6258"Preisigmuller, R. Kindl, H.c 19933-OXOACYL-COA THIOLASE ACETOACETYL-COA AMINO-ACID SEQUENCE CDNA CUCUMIS-SATIVUS FIREFLY LUCIFERASE GENE GLYOXYSOMAL MALATE-DEHYDROGENASE GLYOXYSOME N-TERMINAL SIGNAL NUCLEOTIDE-SEQUENCE PEROXISOMAL 3-KETOACYL-COA THIOLASE PEROXISOME PRE-SEQUENCE PROTEIN IMPORT TARGETING SIGNALhbThiolase Messenger RNA Translated In vitro Yields a Peptide with a Putative N-Terminal PresequencePlant Molecular Biology221 59-66r Apr 6259Preissner, R. Bork, P. 1991,%GLOBULAR-PROTEINS SECONDARY STRUCTUREo^WOn alpha-Helices Terminated by Glycine .1. Identification of Common Structural Features:3Biochemical and Biophysical Research Communications 1802660-665 31 Oct`ZPresley, J.F. Cole, N.B. Schroer, T.A. Hirschberg, K. Zaal, K.J.M. Lippincott-Schwartz, J. 199760ER-to-Golgi transport visualized in living cells Nature 389 81-85 6260,&Presnell, S.R. Cohen, B.I. Cohen, F.E. 19921.7-A RESOLUTION 2.0-A RESOLUTION ALPHA-HELICES AMINO-ACID SEQUENCE BETA-SHEET CRYSTAL-STRUCTURE GLOBULAR-PROTEINS HYDROPHOBICITY PATTERNS REFINED STRUCTURE TERTIARY STRUCTURECHBA Segment-Based Approach to Protein Secondary Structure Prediction Biochemistry314y983-993 4 Feb- 6261,&Presnell, S.R. Cohen, B.I. Cohen, F.E. 1993PJMacMatch - A Tool for Pattern-Based Protein Secondary Structure Prediction.(Computer Applications in the Biosciences93 373-374 Jun 6262Presta, L.G. Rose, G.D. 1988 ALPHA-HELIX Helix Signals in ProteinsTSciencer 240 1632-164111467927B Deinzer1999.Deischel19898$; Deisenhofer1992- Deisenhofer1996&= Deisseroth1992  Dejesu,.-& 36224-Jolles, B. Laigle, A. Liquier, J. Chinsky, L.  1993CIRCULAR-DICHROISM COMPLEXES CONFORMATIONAL CHANGE CROSS-LINKING DEOXYRIBONUCLEIC-ACID DNA DRUG INTERACTION FLUORESCENCE MITOMYCIN-C POLYNUCLEOTIDES RESONANCE RAMAN-SPECTROSCOPY SEQUENCE SPECIFICITY TERBIUM AS A CONFORMATIONAL PROBE Z-DNAXREvaluation of the Structural Modifications Induced by Mitomycin-C on Nucleic AcidsBiophysical Chemistrye462179-185e Apre 3623Joly, J.C. Wickner, W. 1993(!ACIDIC PHOSPHOLIPIDS BACTERIORHODOPSIN MUTANTS CROSS-LINKING ENDOPLASMIC-RETICULUM ESCHERICHIA-COLI SECB INTEGRAL MEMBRANE-PROTEIN MITOCHONDRIAL PRECURSOR PROTEIN PLASMA-MEMBRANE POLYACRYLAMIDE GELS PREPROTEIN TRANSLOCASE PURIFIED COMPONENTS SECA SECY SIGNAL-SEQUENCE TRANSLOCATION PATHWAYThe SecA and SecY Subunits of Translocase Are the Nearest Neighbors of a Translocating Preprotein, Shielding It from Phospholipids EMBO Journal121255-263 Jan,&Joly, J.C. Leonard, M.R. Wickner, W.T. 1994BE2 TRANSITION FUNCTIONAL SITES HIGH-AFFINITY PROTEIN DYNAMICS TRYPTOPHAN FLUORESCENCE Structural Dynamics of the Ca-2+-ATPase of Sarcoplasmic Reticulum - Temperature Profiles of Fluorescence Polarization and Intramolecular Energy Transfer$Biochimica et Biophysica Actar 10282183-199 5 Oct 3625*#Jonas, A. Steinmetz, A. Churgay, L. 1993AQUEOUS-SOLUTION DISCOIDAL COMPLEXES EVOLUTION HIGH DENSITY LIPOPROTEIN LECITHIN-CHOLESTEROL ACYLTRANSFERASE LIPID BINDING MULTIGENE FAMILY PHOSPHATIDYLCHOLINE PROTEIN STRUCTURAL DOMAINSThe Number of Amphipathic alpha-Helical Segments of Apolipoprotein-A-I, Apolipoprotein-E, and Apolipoprotein-A-IV Determines the Size and Functional Properties of Their Reconstituted Lipoprotein Particles&Journal of Biological Chemistrya 2683 1596-1602 25 Jan 3626JCJonas, A. Voneckardstein, A. Churgay, L. Mantulin, W.W. Assmann, G. 19933-DIMENSIONAL STRUCTURE ACTIVATION AMINO-ACID SUBSTITUTIONS COMPLEXES DOMAIN FLUORESCENCE PROPERTIES HIGH-DENSITY LIPOPROTEINS LDL LECITHIN-CHOLESTEROL ACYLTRANSFERASE PHASE FLUOROMETER PROTEINS RECONSTITUTED HDL SEQUENCESb[Structural and Functional Properties of Natural and Chemical Variants of Apolipoprotein-A-Ii$Biochimica et Biophysica Actat 1166 2-3202-210 24 Feb.'Jonassen, I. Eidhammer, I. Taylor, W.R. 1999>7Discovery of local packing motifs in protein structures0*Proteins: Structure, Function and Genetics34206-219o JAH<5Jonasson, P. Aronsson, G. Carlsson, U. Jonsson, B.-H. 1997voTertiary structure formation at specific tryptophan side chains in the refolding of human carbonic anhydrase II Biochemistry36 5142-5148 JAH 2,Jones, T.A. Zou, J.Y. Cowan, S.W. Kjeldgaard 1901voImproved methods for binding protein models in electron density maps and the location of errors in these models`Acta Crystallographica47 (( Pt 2))110-119d 3655 363582Jones, D.H. McMillan, A.J. Fersht, A.R. Winter, G. 1985hbReversible dissociation of dimeric tyrosyl-tRNA synthetase by mutagenesis at the subunit interface Biochemistry2421 5852-5857 8 Oct 3653Jones, T.A. Thirup, S. 1986NGUsing known substructures in protein model building and crystallographyn EMBO Journal54a819-822e Apr 364160Jones, M.D. Lowe, D.M. Borgford, T. Fersht, A.R. 1986ZSNatural variation of tyrosyl-tRNA synthetase and comparison with engineered mutants Biochemistry258 1887-1891 22 Apr 3640*$Jones, M.D. Brand, N.J. Fersht, A.R. 198660Single-stranded M13 DNA: use as a cloning vectorNucleic Acids Research1424 10116 22 Dec 36462,Jones, T.A. Bergfors, T. Sedzik, J. Unge, T. 1988:4The Three-Dimensional Structure of P2 Myelin Protein EMBO Journal76c 1597-1604p Jun 3652Jones, T.A. Schiltz, T. 1989`ZPulsed linear acceleration as a vestibular stimulus in electrophysiological investigations&Journal of Neuroscience Methods2722115-120 Mar 3650 Jones, T.A. Pedersen, T.L. 1989F@Short latency vestibular responses to pulsed linear acceleration("American Journal of Otolaryngology105P327-335Sep-Oct0)Jones, J.D. McKnight, C.J. Gierasch, L.M. 1990Biophysical Studies of Signal Peptides: Implications for Signal Sequence Functions and the Involvement of Lipid in Protein Export0)Journal of Bioenergetics and Biomembranesc223213-231 3648JCJones, T.A. da Cruz e Silva, E.F. Spurr, N.K. Sheer, D. Cohen, P.T. 1990~xLocalisation of the gene encoding the catalytic gamma subunit of phosphorylase kinase to human chromosome bands 7p12-q21$Biochimica et Biophysica Actap 10481t 24-29 30 Jan/NIH/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e/e+ e11e13e14e15e16e17e18e19e1:e1;e1<e1=e1?e1@e1Ae1Be1Ce1De1Ee1Fe1He1Ie1Je1Ke1Le1Me1Ne1Oe1PeP1e1Pe1Pe1Pe1Pe1PeP1eP1eP1eP1e91 Rudolph1991 Rudolph1991j Rudolph1992i Rudolph1992& Rudolph1992u Rudolph1993Rueckert1990 Ruegger1993 Ruff1992v Ruffjamison1993w Ruffle19931 Ruggeri1993+V Ruggero1998 Ruigrok1991 Ruigrok1992-3 Ruiz-Sanz1994+ Ruiz-Sanz1995- Ruiz-Sanz1995 Rukavishnikov1993 Rukmini1993"y Rule19911! Rule1991 Rule1992 Rule1992Rullmannd QUenchingj s s sq s  s" s# s% s-x s- s) s/ s s3 s3 s/ s5P s5Q s5k s5 s5 s5 s s  s  sl s s s  s s  s s7 s s& s s s+i r+l r+q r6 r6v r6 r7 r7 r/roltermous#y6%s11s13s14s15s16s17s18s19s1:s1;s1<s1=s1?s1@s1As1Bs1Cs1Ds1Es1Fs1Hs1Is1Js1Ksi1992  Sacchettini1992- Sacchettini1992- Sacchettini1992. Sacchettini1994. Sacchettini1996* Sacchettini1997% Saccomano1993f Sachdev1993= Sachs1972< Sachs1972; Sachs1972 Sachs1972 5 Sachs1974> Sachs1974 Sachs1974 6 Sachs1975 Sachs1992? Sack1975v@ Sackett1991A Sackett199311DBv13A14A15A16A17A18A19A1:A1;A1<A1=A1?A1@A1AA1BA1CA1DA1EA1FA1HA1IA1JA1KA1LA1MA1NA1OA1PA1QA1RA1SA1TA1UA1WA1XA1YA1ZA1[A1\A1]A1^A1_A1`A1aA1bA1cA1dA1eA1fA1gA1hA1iA1kA1lA1mA1nA1oA1pA1pA1pA1pA1pA1pAClient message sent The Host closed the connection. Retrieving references 22 - 24... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 25 - 27... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 28 - 30... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 31 - 33... Sending messa-6&>/4630X+`.Bolotina, I.A. 1987Determination of the secondary structure of proteins from the circular dichroism spectra. V. The secondary structure of proteins in a "molten globule" state..2,Molecular Biology (USSR) English Translation21 1328-1337 687(!Bolton, W. Cox, J.M. Perutz, M.F.u 1968~Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution331283-297 14 Apr"Journal of Molecular Biology 688Bolton, W. Perutz, M.F. 1970d^Three dimensional fourier synthesis of horse deoxyhaemoglobin at 2.8 Angstrom units resolution Nature 228 271.551-552n 7 NovafJBonagura, C.A. Sundaramoorthy, M. Pappa, H.S. Patterson, W.R. Poulos, T.L.   1996iAn Engineered Cation Site in Cytochrome c Peroxidase Alters the Reactivity of the Redox Active Tryptophan ( )  Biochemistry35 6107-6115Bcytochrome c peroxidase, cation binding site, ascorbate peroxidase     @:Bond, C.J. Wong, K.-B. Clarke, J. Fersht, A.R. Daggett, V. 1997Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment : Description of the folding pathwayVOProceedings of the National Academy of Sciences of the United States of America94 13409-13413d JAH*$Bonifacino, J.S. Dell'Angelica, E.C. 1998.(Protein labeling and immunoprecipitation(!Current Protocols in Cell Biology New York John Wiley & Sons, Inc. 7.2.1-7.2.21 699~Bonmatin, J.M. Genest, M. Petit, M.C. Gincel, E. Simorre, J.P. Cornet, B. Gallet, X. Caille, A. Labbe, H. Vovelle, F. Ptak, M. 1992$2-D-3-D NMR 3-DIMENSIONAL STRUCTURE BACILLUS-SUBTILIS BIOSURFACTANT DEFENSIN-A DISTANCE GEOMETRY CALCULATIONS H 1 NMR ITURIN-A LIPID TRANSFER MAIZE SEEDLINGS MOLECULAR MODELLING NUCLEAR MAGNETIC-RESONANCE PEREGRINA FLESH FLY PHOSPHOLIPID-TRANSFER PROTEIN SARCOPHAGA-PEREGRINA SURFACTINEProgress in Multidimensional NMR Investigations of Peptide and Protein 3-D Structures in Solution - From Structure to Functional Aspects Biochimie74 9-10825-836Sep-Oct2,Bonneau, R. Ruczinski, I. Ysai, J. Baker, D. 2002|8Contact order and ab initio protein structure predictionProtein Science11 1937-1944 JAHjdBonneau, R. Strauss, C.E.M. Rohl, C.A. Chivian, D. Bradley, P. Malmstrom, L. Robertson, T. Baker, D. 2002~MDe novo prediction of three-dimensional structures for major protein families.  "Journal of Molecular Biology 322P 65-78 JAH 700TMBonvin, A.M.J.J. Rullmann, J.A.C. Lamerichs, R.M.J.N. Boelens, R. Kaptein, R.f 1993XR2D NMR 3-DIMENSIONAL STRUCTURE CRAMBIN DISTANCE GEOMETRY ENSEMBLE AVERAGING H-1-NMR ASSIGNMENTS ITERATIVE RELAXATION MATRIX APPROACH LAC REPRESSOR HEADPIECE MODEL-FREE APPROACH NUCLEAR MAGNETIC-RESONANCE OVERHAUSER EFFECT SPECTRA RESTRAINED MOLECULAR-DYNAMICS SIMULATED ANNEALING CALCULATIONS SOLUTION STRUCTURE STEREOSPECIFIC ASSIGNMENTSzEnsemble Iterative Relaxation Matrix Approach - A New NMR Refinement Protocol Applied to the Solution Structure of Crambin154e385-400 Apr0*Proteins: Structure, Function and Genetics 701d^Booker, G.W. Breeze, A.L. Downing, A.K. Panayotou, G. Gout, I. Waterfield, M.D. Campbell, I.D. 19923-DIMENSIONAL STRUCTURES CONFORMATIONS DISTANCE DATA DYNAMICS NUCLEAR MAGNETIC-RESONANCE PROGRAM PROTEIN STRUCTURES SIGNAL TRANSDUCTIONC\VStructure of an SH2 Domain of the p85alpha Subunit of Phosphatidylinositol-3-OH Kinase Nature 358 6388684-687L 20 Aug 702b[Booker, G.W. Gout, I. Downing, A.K. Driscoll, P.C. Boyd, J. 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Curran, A.R. 1999 Membrane protein folding.,%Current Opinion in Structural Biology9115-121  SJEd`"rTropsha%t,S-SYt+t.t.t.t.t.t.t.t1#t1t3t4't5t6t80t8t8t9t8=t8nt8t8ttmanu8t'uardl/allier/ nngttpp%rp%spppw#t%rt%sttwwwbridge s"s s"t s  ssdaleo x x xellpp|y u u uuu`ucuhuVuuuuuuBiochemistry38 9039-9047 JAHx 1916HBEbenbichler, C.F. Roder, C. Vornhagen, R. Ratner, L. Dierich, M.P. 1993AIDS VIRUS FUSION GP36 GP41 HTLV-III/LAV HUMAN IMMUNODEFICIENCY VIRUS INFECTION OLIGOMERIC STRUCTURE PUTATIVE HIV RECEPTOR RECEPTOR SYNTHETIC PEPTIDES T-CELLS TRANSMEMBRANE BINDING PROTEINS TYPE-1 ENVELOPE GLYCOPROTEINb[Cell Surface Proteins Binding to Recombinant Soluble HIV-1 and HIV-2 Transmembrane ProteinsD AIDS7`4n489-495o Apr@.G.2.2.2.2.2+2+2.2.2-2.2.2.2.2.2.P2.2.2.2.2.2.2.2.2.2.2.2.2.2.2.2.2.2/2/2/ 2/222/22/2/2/2/22/22/32-p2/42).2*2/62/72/<2/=2/L2/^2/r2r/2r/2r/2r/2ionships to predict the folding ability of model proteins`0*Proteins: Structure, Function and Genetics33177-203d JAH 1745 Dinsmore, J.H. Solomon, F. 1991DEPENDENT PHOSPHORYLATION DNA EMBRYONAL CARCINOMA-CELLS IDENTIFICATION INVITRO LINE MAMMALIAN NEURONS MICROTUBULE-ASSOCIATED PROTEINS RNA TAUxqInhibition of MAP2 Expression Affects Both Morphological and Cell Division Phenotypes of Neuronal Differentiationi Cell644817-826 22 Feb3Hainfeld19934 Hainzi2002 b Hainzl1994 2 Hainzl200108{ Hainzl2002 c Haire1981 d Hajdu1990 Hajduk199291 Hajduk19996q Hajduk1999/ Hajduk2000" e Hajeer1992 Hajiseyedjavadi1993,' Hajnik19969 Hajra1993Hakomori1992# Haldar19922. Hale19979 Halestrap1992 Halevy1990 f Halevy1990  Halevy1991 Haley1991I Haley1993%Halfmann1990.  Halfon1996 g Halford19928 Halgand1999 h Halgren1992( Haliloglu1997 i Hall1980vP Hall1980v Hall198080 Hall19828 l Hall1982v k Hall1982v j Hall1982v Hall19898 m Hall1989v= Hall19919 m Hall19919 Hall1992i n Hall1992v Hall19922 Hall19921 Hall19931 Hall19931 Hall19939# Hall19939 Hall19939) Hall1995v0 Hall20013 Hall20028 Hall20027 Hall2003Hallberg1990 Hallberg19929 pHallberg1993 pHallberg1993 oHallberg1993  Halle1991, Halle1999- Halle19993 Halle20028 Halle2003Hallenga1993)Hallenga19976Hallenga19976DHallenga20010  Hallewell1989 Hallewell1990 Hallewell1992 Hallewell1992Halligan1993Halligan19936; Hallock1998#Halloran19928 Halsall1991 Halsall1993 Halsall1993 S Haltia19921 T Haltia19939G Haltiwanger1982 : Halverson1990 q Halverson1991 ; Halverson1992E Halvorson19754 Ham2002 Hamada1991  Hamada19919 r Hamada1993 !_ Hamada1993 Hamada19939 Hamada19939 s Hamada1996 6< Hamada1996& Hamada1997-r Hamada19999/_ Hamada2000 3` Hamada2002<N Hamaguchi1990 Hamaguchi1990O Hamaguchi1991 Hamaguchi1992 t Hamalainen1991 Hamamoto19939\ Hamann1998.9] Hamann1999.Hamasuna1991/ Hamel2000 Hamet1992c Hamiche19943 Hamill19962) Hamill1997<. Hamill1999/ Hamill20002& Hamill2000<3 Hamill2000YHamilton19711 Hamilton19888 qHamilton1991 uHamilton1991 vHamilton1991 wHamilton1992[Hamilton1992Hamilton19929 Hamilton1993Hamilton1993 yHamilton1993 xHamilton1993.Hamilton19966*Hamilton19979$ Hamm19919 Hamm19939 Hamm1993i* Hamm1997i/ Hammack2000 Hamman19955+i Hamman1997* Hamman1998 6 Hamman19988m Hammarback1990 z Hammarback1991 L Hammarberg1991 0t Hammarstrom20011 Hammarstrom20027 Hammarstrom2003 { Hammen1991 | Hammen1996 } Hammen1996 # Hammen19966 Hammerling1993  Hammerling1993 "Q Hammock19932* Hammond1955$t Hamodrakas1992 _ Hampl19937o Hamuro20027p Hamuro2002 ~ Hamy1993v) Hamy19939  Han1992  Han1992  Han1992 Han1992  Han1993 Han1993 Han1993% Han1993# Han1993+ Han19981L Han20012 Han20015 Han20035 Han2003% Hanada19949  Hanada1996 #Hanafusa19922Hanafusa1993 Hanai19938 Hanberger1991 Hanby1993  Hancock1991 Hancock19939 Hancock19999 Hancock2004 Handa1993 Handel19929  Handel1993  Handel1993 Handel19939 Handel19951 Handel1996+ Handel1998 .F Handel19991.P Handel199912O Handel19999( Handel?1997+AHandford1998 Handschin1991$Handschumacher1990Handschumacher1990 Hanesworth1993 Hangauer1984z Hanger1991 { Hanger1991  Hanger1991  Hanger1992  Hanigan1991  Hanigan19920 Hanin1987 Hanis1990 Hanley1989 B Hanley1990 D Hanley1991  Hanley1993 S Hanley-Way1981  Hanlon1992 '- Hanlon19929  Hanlon1992  Hann1989v  Hann1991v  Hann1992v Hann19944P Hannah1993 Hannavy1993 Hannavy19934 Hannemann2002  Hanover1992  Hansbro1992  Hansbrough1991  Hansbrough1992' Hansen1976 Hansen1990  Hansen1992  Hansen19929 Hansen1992P Hansen1992  Hansen1993  Hansen1993  Hansen19939'= Hansen19933  Hansen1994 * Hansen1997 8 Hansen20002 Hansen200208 Hansen2003 Hansma19949 Hansma199494 Hansma200204 Hansma200209Hansmann1993l  Hanson1992  Hanson1992  Hanson1992 Hanson19939H Hanson1993  Hanson19939& Hanson1993 & Hanson19979 Hanssens1991 YHanssens19933# Hanssens19941! Hansson1985 Hantgan1990( Hantzbrachet1991 Hanyu1992  Hanzlik1991  Hao1993+B Hao1998,C Hao1998) Haque1996) Haque1997  Hara1990v% Hara19921w Harada19919Harakuge1993  Haran1992 Hamaguchi1991 Hamaguchi1992 t Hamalainen1991 Hamamoto1993Hamasuna1991c Hamiche1994YHamilton19711 Hamilton19888 qHamilton1991 uHamilton1991 vHamilton1991 wHamilton1992[Hamilton1992Hamilton19929 Hamilton1993Hamilton1993 yHamilton1993 xHamilton1993.Hamilton19966*Hamilton19979$ Hamm19919 Hamm19939 Hamm1993i* Hamm1997i Hamman19955* Hamman1998 m Hammarback1990 z Hammarback1991 { Hammen1991 | Hammen1996 } Hammen1996 # Hammen19966 Hammerling1993  Hammerling1993 "Q Hammock1993$t Hamodrakas1992 _ Hampl1993 ~ Hamy1993v) Hamy19939  Han1992  Han1992  Han1992 Han1992  Han1993 Han1993 Han1993% Han1993% Hanada19949  Hanada1996 #Hanafusa19922Hanafusa1993 Hanai1993 Hanby1993  Hancock1991 Hancock1993 Handa1993 Handel19929  Handel1993  Handel1993 Handel19939 Handel19951 Handel1996( Handel?1997 Handschin1991$Handschumacher1990Handschumacher1990 Hanesworth1993 Hangauer1984z Hanger1991 { Hanger1991  Hanger1991  Hanger1992  Hanigan1991  Hanigan19920 Hanin1987 Hanis1990 Hanley1989 B Hanley1990 D Hanley1991  Hanley1993 S Hanley-Way1981  Hanlon1992 '- Hanlon19929  Hanlon1992  Hann1989v  Hann1991v  Hann1992v Hann19944P Hannah1993 Hannavy1993 Hannavy1993  Hanover1992  Hansbro1992  Hansbrough1991  Hansbrough1992' Hansen1976 Hansen1990  Hansen1992  Hansen19929 Hansen1992P Hansen1992  Hansen1993  Hansen1993  Hansen19939'= Hansen19933  Hansen1994 * Hansen1997  Hansma19949 Hansma19949  Hanson1992  Hanson1992  Hanson1992 Hanson19939H Hanson1993  Hanson19939& Hanson1993 Hanssens1991# Hanssens19941 Hantgan1990( Hantzbrachet1991  Hanzlik1991  Hao1993) Haque1996) Haque1997  Hara1990v% Hara19921w Harada19919Harakuge1993  Haran1992ran19921oJ1pa1sa1ta1xa1ya1|a1}a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1aa1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a0ma1a/a1a1a1a1a1a1a1a%("$% 뷥 ! "* (  ("*$%%*  췯  !*$ ﯽᵀ" 0"$ 巪*$! .! ( ! "%% $"!*H7310 r0-50.30(010+0.050001`142345576 79892a2 0 030800(0*%0)0>0202z080 0 01~122_3~455867_8993344*11511b1)1%C0message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 10 - 12... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 13 - 15... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 16 - 18... Sending message to server... Connecting to host... Client message sent The Host cl2Uid2P2P2P2P2P2P2P2!P2 P2"P2$P2%P2)P2(P2'P2&P2+P2-P2.P21P22P23P24P25P26P27P28P29P2:P2;P2<P2=P2>P2?P2BP2@P2CP2DP2EP2IP2HP2GP2FP2JP2KP2NP2MP2LP2PP2QP2RP2TP2SP2VP2XP2XP2XP2XP2XP2XP2XP2XP2XPage to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 4 - 6... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Paused Aborted Connecting to host..N8And8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a6a8a8a8a8a8a)a;a)$a)a)a5a&a)Ha)a)%a)&a)-a+[a+da'Oa'Ja+ia+la)a'Ma+wa)a'Ta+xa+|a+}a+~a+a+a+a+a+a+a)Fa11'a13'a15'a1?'a1A'a1D'a1E'a1J'a1O'a1T'a1U'a1W'a1Z'a1_'a1a'a1b'a1e'a1f'a1s'a1t'a1v'a1x'a1'a1'a15'a1?'a1A'a1D'a1E'a1J'a1O'a1T'a1U'a1W'a1Z'a1_'a1a'a1b'a1e'a1f'a1s'a1t'a1v'a1x'a1'a1'ama4.Protein structure prediction: Playing the fold218279-281$Trends in Biochemical Sciences 3358Hubbs, A. Roy, H.8 1992ESCHERICHIA-COLI EXPRESSION GENES HIGHER-PLANT CHLOROPLASTS PEA-CHLOROPLASTS PROTEIN-SYNTHESIS RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE TRANSCRIPTION TRANSLATIONxqSynthesis and Assembly of Large Subunits into Ribulose Bisphosphate Carboxylase Oxygenase in Chloroplast ExtractssPlant Physiology 100r1272-281 Sep mU2222:2W2222222t2222222222222/2Q2P2R2T2b222U2r22222222 2'2,2X2h2s2v22/21202322 -2 Q2 i2 2 2 2 2 2istryP 2663i 1804-1808e 25 Jan 152981Dahlmanwright, K. Wright, A.P.H. Gustafsson, J.A.A 1992DIMER FORMATION DIMERIZATION ESTROGEN-RECEPTOR GENE HEAT-SHOCK PROTEIN NEGATIVE REGULATION PROGESTERONE-RECEPTOR RESPONSIVE ELEMENT STEROID-BINDING THYROID-HORMONE RECEPTORDeterminants of High-Affinity DNA Binding by the Glucocorticoid Receptor - Evaluation of Receptor Domains Outside the DNA-Binding Domain Biochemistry3137 9040-90447 22 SepTOehlerplil'lofsenn)Yne P86sch0tt/PfppNNNN N N N)NNNN(NNNNNNNNNNNNNN#N$N%N&N'N(N)N*N-N/N.N0N1N2N3N4N5N6N7N8N:N<N=NedemaThlerlil'lofsennY)neӖ P86sch0ttP/fppNNNN N N N)NNNN(NNNNNNNNNNNNNN#N$N%N&N'N(N)N*N-N/N.N0N1N2N3N4N5N6N7N8N:N<N=N0 ,1998 DecshbA  881d]Bryant, C. Strohl, M. Green, L.K. Long, H.B. Alter, L.A. Pekar, A.H. Chance, R.E. Brems, D.N.i 1992H-1-NMR ASSIGNMENTS MAIN-CHAIN NATIVE HUMAN INSULIN PHOTO-CIDNP PROINSULIN PROTEINS RECEPTOR INTERACTIONS RESOLUTION RESONANCES SEMISYNTHESISc\UDetection of an Equilibrium Intermediate in the Folding of a Monomeric Insulin Analogt Biochemistry3125 5692-56988 30 Jun 884"Bryant, S.H. Lawrence, C.E.c 19933-DIMENSIONAL STRUCTURE CONFORMATIONAL ENERGY CRYSTAL-STRUCTURE EGLIN-C FOLDED PROTEINS GLOBULAR-PROTEINS KNOWLEDGE-BASED PREDICTION MEAN FORCE PROTEIN FOLDING RESIDUE CONTACTS SOLVENT ACCESSIBILITY SUBTILISIN CARLSBERGd\UAn Empirical Energy Function for Threading Protein Sequence Through the Folding Motife161 92-112 May0*Proteins: Structure, Function and Genetics 88082Bryant, B.P. Leftheris, K. Quinn, J.V. Brand, J.G. 1993AMINO-ACIDS CHANNEL CATFISH ICTALURUS-PUNCTATUS L-ALANINE L-ALANINE ANALOGUES LIGAND BINDING ASSAY SENSATION SITES SPECIFICITY STIMULUS STRUCTURE ACTIVITY TASTE RECEPTORc`YMolecular Structural Requirements for Binding and Activation of L-alanine Taste ReceptorsA Amino Acidst4 1-2h 73-88e>8Bryngelson, J.D. Onuchic, J.N. Socci, N.D. Wolynes, P.G. 1995RKFunnels, pathways, and the energy landscape of protein folding: a synthesis0*Proteins: Structure, Function and Genetics21167-195  JAHXRBryson, J.W. Betz, S.F. Lu, H.S. Suich, D.J. Zhou, H.X. O'Neil, K.T. DeGrado, W.F. 1995,&Protein design: a hierarchic approach.Scienceg 270935-941 design SJEt82Brzovic, P.S. Meza, J.E. King, M.-C. Klevitt, R.E. 2001ztBRCA1 RING domain cancer-predisposing mutations: Structural consequences and effects on protein-protein interactions&Journal of Biological Chemistry 276A 41399-41406 JAH| DIvErsIty ib ii i i i  i// i+t i0v i2 i+ i i{ i  i% i+t i6 i6 i6 i6 i7K i7 i8} i8 i5V' i&/ide7:ddiiing&2sWsionx+x 8x ?tttSttt ttBt t!Wt!t$tt5t7t7:t7t 8tttt7:t8t&t+xt+t1`'t1't1't1't2't2't3't4z't5D't5H't5M't5't5't5't5't3[H3Ua3ga3la3ma3wa3ua3na3a3a3a3a3a[a$a"a3a3a3a3a3a3a3a3a3a3a3a3a3a3a3a4a4a4a4a4a4#a4+a4(a4&a4Ha4<a4Ma4Ra4Sa4da4ba4aa4_a49a4a4wa4ya4za4}a4a4a4a4)a4a4a1a(a#aAdams, M.W.W. Park, J.B. Zhou, Z.H. Bax, A.1 1992LECD-113 HG-199 HYDROGEN BONDING J-COUPLING NMR RUBREDOXIN SPECTROSCOPYXQuantitative Measurement of Small Through-Hydrogen-Bond and Through-Space H-1-Cd-113 and H-1-Hg-199 J-Couplings in Metal-Substituted Rubredoxin from Pyrococcus-Furiosus"Journal of Biomolecular NMRc2s5527-533 Seps 627 Blake, G.A. 1992"Hydrogen Bonding - ResponseScience 2589 5081381-382 16 Oct%L%1%1(1%1%1%1%1%1%1%1%1%1%1%1&1& 1&1&1&1+1&&1&/1&11&51&71&61&D1&A1&?1&I1&P1&O1&N1(1*1&T1&V1&Z1&`1&a1&b1&1&x1&w1&v1&u1&1&1&1'!1'"1+L1+S11X1X1X1X1X1X1X1X1X1 E6h\@~h 0@<'MOfcNNNN+wN)N)NCN'TN+xN+yN+zNtNWNN+|N+}N+~N+N SN+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N+N NON{NN# Chemistry# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I# I$ I$  I$  I$ I$ I$! I$0 I$@ I$Q I$w I$} I$ I$ I$ I$ I$ I$ I$ I$ I$ I$ I$ I$ I$ I$ I% I%' I%- I%2 I%6 I%B I%Z I%\ I%b I%e I%q I%q I%q I%q I%q I%q I%q I%)BInding%*o%6o%Io%ro%so+1o%o%o%o%o%o%o%o%o%o%o%o&o&o&o&o+o&o&%o&8o&>o&Mo&Jo&Io&Oo&To&o&to&o&o)o'o'o'!o+Ho+Lo+No+Oo+Vo)%o)&o)+o)-o)#o)*o+]oo%oo+fo'Jo'Jo'Jo'Jo'Jo'Jo'Joa* @8 xAmiNo P P P P P P P P TransITione Y Y Y Y Y Y Y Y) Yf Y Y  Y A Y P Y u Y  Y  Y  Y  Y  Y  Y  Y  Y  Y : Y 9 Y  Y  Y  Y* Y  Y\ Yo Y Y Y Y Y: Ys Y# Y Y Y Y Y Y Y( Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yn Yeeeenkel g g g3g gilitymentfSGER-RNA NEUROTRANSMISSION PERTUSSIS TOXIN PROSTAGLANDIN-E2 VASOPRESSIN2 Isoforms of the EP3 Receptor with Different Carboxyl-Terminal Domains - Identical Ligand Binding Properties and Different Coupling Properties with G(i) Proteins&Journal of Biological ChemistryS 26842 2712-27182 5 Feb2 p ; 7602*#Sugawara, T. Kuwajima, K. Sugai, S. 19912222222u222222221222222222222222222 2Z2222)222222222]2c2N2222L2X2222 222m2m2m2 Academy n! n!n!%n!/n!Cn!Xn!Yn!n)n!n!n!n!n"n"n"!n"_n"n"n"n"n"n#n#n#n#n#.n#En#fn#n#n$n$n$%n$)n$*n$>n$Zn$bn$fn$n$n$n$n$n$n) n$n$n$n%n%(n%,n&n%tn*n%n%n%n%n%n =269 0 )0 0 X0 0&0e00000000000000K0u00A0M0M0W00000"0$0$^0$\0$0%W00,K0,S0.V0001 00[0607080809b0000.00 O0 0 0 0 0100000ki1993 ) Czajkowsky1993 j Czar1992i Czar1992k Czar19931Czarnota1992'JCzarnota19949 Czech1992 Czech1992 Czech1993L Czernik1992 Czernik1993# Czernilofsky1993 Czisch1993 > Czisch19931- Czjzek1999i; Czurylo1993< Czworkowski19948D'Andrea2003', d'Avignon1989- d'Avignon1990 d'Avignon1991? d'Avignon1995- D'Silva1999e"x EXplained6& i6 i6 i7A i8f ieing6 s3s)nn-n6n6n8{n8n#nationi  i, s0h s+~ s+ s0 s6 s6 s6 s7 s8[ s-@ s> i8 i4)icablei it,l9#l91l9*l92l6l68l6l8;l8dl8l xlyo y o& o8oit8a)Gation7 e7 e7 e eds< s s6D s7: s7:ing7: sssCCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECCECŀCECCECCECCECрCECCECCECـCECCECCECCECCECCECCECCECCECCECCECCECCECCEDCEDCEDCED@CEDCEDCED CED CED CED@CEDCEDCEDCEDCED@CEDCEDCEDCE6folding6r6r6r6r6r6)r62r64r68r69r6?r6@r6Cr6Gr6Rr6Wr6hr6nr6tr6wr6|r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r6r7r7r7r7r7r7 r7 r7r7r7r7r7r7r7r7!r7#rhe ER membrane. SRbeta can be cross-linked to a 21 kDa ribosomal protein in its empty and GDP-bound state, but not when GTP is bound. GTP binding to SRbeta is required to induce signal sequence release from SRP. This is achieved by the presence of the translocon, which changes the interaction between the 21 kDa ribosomal protein and SRbeta and thereby allows SRbeta to bind GTP. We conclude that SRbeta coordinates the release of the signal sequence from SRP with the presence of the translocon.y'nhStruct%Receptor%o%o%o%o%o&>o&Mo&Lo&uo&to&o&o)3o)1o+Joroooo)2o+ro+|oOo,.o,2o*o,Mo,Qo,o,o&o$o$o%lo.To/o/%o/&o.|o/oto0Uo0vo0xo1o1'oo@o0o0o1(o1o2~o2o2o2o2o2o2o2o2o3o2ZUid2YP2[P2\P2]P2_P2^P2`P2aP2bP2dP2cP2eP2fP2gP2iP2hP2jP2nP2mP2oP2pP2qP2rP2sP2tP2uP2vP2wP2xP2yP2zP2{P2|P2}P2~P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P2P 050789$?9N88:88J88z8 1 t1&00"00 014f'14e'14d'11 222 2}222>2333 S34)488556678$?89%99 99X9l1000$`0,0 ,0400$[0111224 ȥ   Curr Opin Struct Biolp101p 46-51 10679459{http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=10679459 http://www.biomednet.com/article/sba104z'Section of Structural Biology, Institute of Cancer Research, Chester Beatty Laboratories, London, SW3 6JB, UK. l.pearl@icr.ac.uk!. ȤЫ 0CHLPearl ProdromouȫpȧgӁ02000 Prodromȧ 9 8 7 6 2 1 0 / .f -| , + ** )n (2JDHellman, R. Vanhove, M. Lejeune, A. Stevens, F. J. 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Qureshi, M.N.m 1993AIDS RETROVIRUS CYTOPLASMIC DOMAIN ENVELOPE GLYCOPROTEIN HIV INFECTION PHORBOL-MYRISTATE ACETATE SEQUENCE IDENTITY SOLUBLE CD4 SYNTHETIC PEPTIDE T4 ANTIGEN TRANSMEMBRANE PROTEINrlA Peptide Inhibitor of Human Immunodeficiency Virus Infection Binds to Novel Human Cell Surface Polypeptides&Journal of Biological Chemistryo 26820 15291-15297d 15 Jul 3124 Hendrick, J.P. Wickner, W. 1991COAT PROTEIN CYTOPLASMIC MEMBRANE LAMBDA-DNA PHOSPHOTRANSFERASE SYSTEM PRECURSOR PROTEINS PRO-OMPA SUGAR-TRANSPORT TRANSLOCATION ATPASE TRIGGER FACTOR VESICLESPSecA Protein Needs Both Acidic Phospholipids and SecY/E Protein for Functional High-Affinity Binding to the Escherichia-Coli Plasma Membrane&Journal of Biological Chemistry 26636 24596-24600` 25 Dec 3123D>Hendrick, J.P. Langer, T. Davis, T.A. Hartl, F.U. Wiedmann, M. 1993CROSS-LINKING DOMAINS ENDOPLASMIC-RETICULUM MEMBRANE HSP70 PREPROLACTIN PROTEIN TRANSLOCATION SEQUENCE SIGNAL RECOGNITION PARTICLE SUBUNITS YEAST HOMOLOGlfControl of Folding and Membrane Translocation by Binding of the Chaperone DnaJ to Nascent Polypeptides9021 10216-10220P 1 Nov0VOProceedings of the National Academy of Sciences of the United States of America Hendrick, J.P. Hartl, F.U. 1993<5Molecular chaperone functions of heat-shock proteins.$Annual Review of Biochemistryp62349-384 Hendrick, J.P. Hartl, F.U. 1995:3The role of molecular chaperones in protein foldingi9s15 1559-1569d FASEB Journal 3128 Hendrix, R.W. 1979\VPurification and Properties of groE, a Host Protein Involved in Bacteriophage Assembly 129375-392S"Journal of Molecular Biology2 64123342076244 555 8 8666 777888 8g999-2020272202022 2 Q2 2 u2&0,0070001223[36068666645[63038888-7-888-999e average coordinates of the backbone atoms of the core residues of E. coli cyclophilin have an rms deviation of 1.44 A, with conserved regions in the crystal structure of unligated human T cell cyclophilin [Ke, H. (1992) J. Mol. Biol. 228, 539-550]. Four regions proximal to the active site differ substantially and may determine protein substrate specificity, sensitivity to cyclosporin A, and the composite drug:protein surface required to inhibit calcineurin2DBv2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A1jA1VA2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A2A1>A2A2A2A2A2A2A2A2A2A2A2A2A2A7R METABOLISM7W t7X t7] t7^ t7_ t7` t7a t7b t7c t7d t7e t7g t7h t7j t7k t7l t7m t7n t7o t7p t7r t7s t7t t7u t7v t7w t7y t7z t7{ t7| t7} t7~ t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t7 t ( X c@0    c@ ). X c@0   c@ " X c@0   c@ ." X c@0 | s c@ Fs+ X c@0  s1 c@ !te/2 X c@0  ;6e[6 c@ !|e X7| Chemistry7} k7~ k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k7 k%'%m++++++5.D$+*g+T(() + ~@99+#+#+#+#ccccccccccccc&&&dddddd&&&&&&&&&&&&&&&&&&&&&&&;;&;;;;;;;;;;;;;(((lllllllllllllleeeeeeeeeeeeiiiiiiiiiiiiiiiggggggggggggg""""""""           SACCHAROMYCES> eD e\ ee e e e eL e_ e e e e e e e e" e e e e e e e e e" eI eQ e e e e e e e e e e  e ey ez e~ e e e er eu ew ez e e eA e e e e e e e e x e z eHLFBychkova, V.E. Dujsekina, A.E. Fantuzzi, A. Ptitsyn, O.B. Rossi, G.-L. 1998ZSRelease of retinol and denaturation of its plasma carrier, retinol-binding protein.Folding and Design3 285-291 SJELEBycroft, M. Matouschek, A. Kellis, J.Y., Jr. Serrano, L. Fersht, A.R.o 1990PJDetection and characterization of a folding intermediate in barnase by NMR Nature 346t488-490 JAHDunlap. C.A. Tsai, M.-D. 2002bUse of 2-aminoG000+0`00000 0 0 u0 0U0\0)0C00000,0g00)00w0W000!0#0$0&u0+d0'J06!0_0 0$r0)00)0700 0 0 0&0 0)0)000000000 0 0 0 @ PJ$REVIEWe)&e6e6e7e7e7e7e7e7e7e8)e88e8Geee "e e5e,e-e)e++e01e4e4e4e4e4e4e4e5e5e5e5e5e5e5e5e6e6e6e6/e62e65e66e6?e6Le6me6oe6e6e6e6e61991VONMR spectroscopy and protein folding: studies of lysozyme and alpha-lactalbumind 161167-181 CIBA Foundation Symposium Dobson, C.M. 1992*#Resting places on folding pathways.`Current Biology2343-345 Dobson, C.M. 1992<6Unfolded proteins, compact states and molten globules.2 6-12,%Current Opinion in Structural Biology Dobson, C.M. 1993Flexible friends.Current Biology3530-532GEneraltt-t5t]t\t it!Mt!t":t"t"t#t#Ct#t#t%tt(tt ht |t at tat3t;ttttt!t!t$t%t&t&xt-tt$ltctt"ttt Yt6i4i`iiiOiiijii#i$&i).i0i)/i4)i6`withg6aD6bD6eD6fD6gD6hD6jD6mD6nD6pD6sD6tD6uD6vD6wD6xD6{D6}D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6D6QUery6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s6s7s7s7s7s+qbetween'Pzoz+rz+xz+{z+|z+~z+z+z+z+zzNzsz+z+z+tz#z0z0z0z#zz+ z0z0z4)z4z&z52z5z5z5z5z6z6z6 z6z6z6z6z6z6z6z6!z6#z6&z6(z6-z61z63z64z67z68z6=z6@z6Cz6Dz6Hz6Kz6Mz6Pzuggests that native DHFR exists in equilibrium with at least one conformer which is recognizable by chaperonin 60. Binding studies with S-35-labeled DHFR support these conclusions and further demonstrate that DHFR competes for a common saturable site with another protein (ribulose-1,5-bisphosphate carboxylase) known to interact with chaperonin 60.Ad^Complex Interactions Between the Chaperonin-60 Molecular Chaperone and Dihydrofolate Reductase Biochemistry3040 9716-97230 8 Oct9. Cregut19996 Cregut1999) Creighton1978  Creighton1980 Creighton1980 l Creighton1980 Creighton1980 Creighton1980 Creighton1980 Creighton1980  Creighton1981 G Creighton1981  Creighton1981 Creighton1981 Creighton1981 Creighton1981  Creighton1982 G Creighton1983  Creighton1983 Creighton1983 Creighton1983 Creighton1984 Creighton1984 I Creighton1984 H Creighton1984 Creighton1984 Creighton1985 J Creighton1985 Creighton1986 Creighton1986 Creighton1986I Creighton1986 Creighton1987 Creighton1987 Creighton1987 r Creighton1987 Creighton1988 Creighton1989 Creighton1989 Creighton1990 Creighton1990n Creighton1991m Creighton1991'E Creighton1991 Creighton1991 Creighton1991 Creighton1991 Creighton1991 Creighton1991#% Creighton1991#$ Creighton1991o Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992& Creighton1992#& Creighton1992 Creighton1992p Creighton1993 Creighton1993 Creighton1993  Creighton1993v Creighton1993u Creighton1993#' Creighton1993 Creighton1993 Creighton1993 Creighton1993 Creighton1993q Creighton1994 Creighton1994 Creighton1994  Creighton1994" Creighton1994,J Creighton199462 Creighton1994 Creighton1995( Creighton19970' Crema2000& Crespi19922 Cresswell1991$N Cresswell1992 Cresswell1993D Cresswell1995 Creuzet1991 Crickmore1992 Crine1993  Crippen1991 Crippen1992FCrisanti1980_Crisanti19878 Crisma19911" Crisma19919" Crisma19921 Crisma19929 Crisma19922 Crisma19929  Crisma1993 "? Crisma19933 Crisma1993o/6 Cristobal1999W Critchley1992  Critchley1992tCrivelli19933hCrocenzi1991 Crocker1991+SCrofford1998  Crombie1992 Cromie19933Crompton1989Crompton199098h Cronan1990 Cronan1991 6 Cronan1996.< Cronan1999t  Cronet1993 = Cronet1996 1 Crooke19868 Crooke1988   Crooke1988 x Crooke1988/ Crooke19891u Crooke1990 - Crooks1997 3 Croonquist2001 Crosby19911) Cross1985 Cross1991 Cross1991 Cross1992&D Cross1992 Cross1993 Cross1993 Cross1993 Cross19932 Cross19936{ Cross1993+ Cross1994)Crothers1992/ Crouch20000 Crow1982v Crowe19901 Crowhurst20024, Crowhurst20025 Crowhurst20035 Crowhurst2003 Crowley1991 Crowley1993 Crowley19943Q Crowley2002UCrowther19696,Crowther1981Crowther1990Crowther1991 2Crowther1991Crowther1992 5Crowther19929Crowther1992 6Crowther1993*Crowther1998Crumpton1989+Crumpton19922, Cruz19931 Cruzalegui1992 S Crystal1991' Csaszar1993Cserhati1992Cserhati1993Csermely1991Csermely1993 Csizmadia1991' Csizmadia1993 Cuatrecasas1967 Cuatrecasas1967 Cuatrecasas1967 Cuatrecasas1967  Cuatrecasas1967  Cuatrecasas1968$ Cuatrecasas1968# Cuatrecasas1968" Cuatrecasas1968! Cuatrecasas1968' Cuatrecasas1969& Cuatrecasas1969% Cuatrecasas1969  Cuatrecasas1969 Cuatrecasas19697 Cubarsi2000( Cudd1982v Cudd199398R Cudic2002 Cuello19939) Cuenoud19933S Cuesta1999< Cueva1992* Cuezva1993 92* Cuezva1993 n1980  Creighton1981G  Creighton1981  Creighton1981 Creighton1981 Creighton1981 Creighton1981  Creighton1982G  Creighton1983  Creighton1983 Creighton1983 Creighton1983 Creighton1984 Creighton1984I  Creighton1984H  Creighton1984 Creighton1984 Creighton1985J  Creighton1985 Creighton1986 Creighton1986 Creighton1986I Creighton1986 Creighton1987 Creighton1987 Creighton1987r  Creighton1987 Creighton1988 Creighton1989 Creighton1989 Creighton1990 Creighton1990n Creighton1991m Creighton1991E' Creighton1991 Creighton1991 Creighton1991 Creighton1991 Creighton1991 Creighton1991%# Creighton1991$# Creighton1991o Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992 Creighton1992& Creighton1992&# Creighton1992 Creighton1992p Creighton1993 Creighton1993 Creighton1993 Creighton1993  Creighton1993v Creighton1993u Creighton1993'# Creighton1993 Creighton1993 Creighton1993 Creighton1993 Creighton1993q Creighton1994 Creighton1994 Creighton1994  Creighton1994" Creighton1994J, Creighton1994 Creighton1995( Creighton1997'0 Crema2000 & Crespi19922 Cresswell1991N$ Cresswell1992 Cresswell1993D Cresswell1995 Creuzet1991 Crickmore1992 Crine1993  Crippen1991 Crippen1992FCrisanti1980_Crisanti19878 Crisma19911" Crisma19919" Crisma19921 Crisma19929 Crisma19922 Crisma19929  Crisma1993 ?" Crisma19933 Crisma1993o6/ Cristobal1999W Critchley1992  Critchley1992tCrivelli19933hCrocenzi1991 Crocker1991S+Crofford1998  Crombie1992 Cromie19933Crompton1989Crompton19909 Cronan1991 <. Cronan1999t  Cronet1993 = Cronet1996 1 Crooke19868 Crooke1988  Crooke1988 x Crooke1988/ Crooke19891u Crooke1990 - Crooks1997 3 Croonquist2001 Crosby19911) Cross1985 Cross1991 Cross1991 Cross1992D& Cross1992 Cross1993 Cross1993 Cross1993 Cross19932 Cross1993+ Cross1994)Crothers1992/ Crouch20000 Crow1982v Crowe19901 Crowhurst2002 Crowley1991 Crowley1993 Crowley1994Q3 Crowley2002UCrowther19696,Crowther1981Crowther1990Crowther19912 Crowther1991Crowther19925 Crowther19929Crowther19926 Crowther1993*Crowther1998Crumpton1989+Crumpton19922, Cruz19931 Cruzalegui1992 S Crystal1991' Csaszar1993Cserhati1992Cserhati1993Csermely1991Csermely1993 Csizmadia1991' Csizmadia1993 Cuatrecasas1967 Cuatrecasas1967 Cuatrecasas1967 Cuatrecasas1967  Cuatrecasas1967  Cuatrecasas1968$ Cuatrecasas1968# Cuatrecasas1968" Cuatrecasas1968! Cuatrecasas1968' Cuatrecasas1969& Cuatrecasas1969% Cuatrecasas1969  Cuatrecasas1969 Cuatrecasas1969( Cudd1982v Cudd19939 Cuello19939) Cuenoud1993S3 Cuesta1999<  Cueva1992* Cuezva1993 1993 b,.163364,.5 5"6667o77 78889/t3+96/t3$}6&4C99c0 W0 0$0)0*k0c000t00 0 0 40"0#0&0&u0!:07S0)Z0 000V0]0%006G00 000070$}01/p243 h4*4"40171/p1/r24/r2,D3,D8.9 5&=7-O.OfOMORULINS[SX*yemuraqVerskiiIyOfOMORULINS[SX*yemura"Vqaf0/16424199938andB BiochemistrybyCD denaturedDobsonfield gradient Grimshaw HydrodynamicJJonesKLM measurednativeNMRof proteinspulseradii ReceveurSSmith techniquesVWilkinsf@p[&1992&3&3&3&3&3'3'3'3'3'!3'"333%73333333+3+3+3+3 3 E3F33"333 3>3,3l333 3%3)3!9333333A3q3p3M33p33-3{3 C3 F333333/ Structure/ s/ s/* s- s/+ s/, s8 s-] s// s/4 s( s/A s/D s/F s/G s/N s/[ s/r s/t s- s. s. s. s/B s- s/0 s+ s/ sE s( s+3 s+t s/ s/ s/ s/ s/ s/ s/ s/ s/ s/ s/ s/ s- s0 s s sy st sv sw s ss s/? s0  s0 s0 s/ sp sp sp s0KK0Ra0Sa0Ta0Ua0Wa0Na0La-a)a/a.a0ia.aa0wa0a0a0a0a0a0ya0|a0a0a0a0a0a0a0a0a0a0a0a0a0a0a0a#a1a1#a/9a1aa1'a.a0a1&a1$a1/a1a0aa)Fa0a1%a17a1;a1Fa1Ha1Ta1Wa1ca1ca,oni,b,R,,,,-%,&=, C -X-Z-^-c-y-}---------O--...$#).B.M.`-Q.x.v.,...+G-../ M//#/8($Wange$i$ i$ i$ i$ i$ i$i*}i&i$i)i*Ji$i%i%i%i&i+Hi+i*i+-i+,i,Di*i,wi,i,i*i-i-i.i. i.!i.;i.>i.?ii.Vi.Zi.i.i/i-]i+i/i/i0i0i0i0i+ i1i1$i$i/-i0i1@i1Mi2i2!i2i2i3i3i3:i37i3Ai3i4i4i5Ii5i5~i5i5i6vi6i6i70i7;i7<i7Ci7Ii7i7i7i8 i89i8Ii8Yi8i8i9\i9]i8i8Y'i-/ikari$ikawathe connection. 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Farrell, Cathy Langley, Kenneth H. Fournier, Maurille J. 1984voPhysical properties of the E. coli 4.5S RNA: first results suggest a hairpin helix of unusual thermal stabilityNucleic Acids Research124p 2019-2034 JLF 736.(Bourne, H.R. Sanders, D.A. McCormick, F. 1991ADP-RIBOSYLATION ALPHA-SUBUNIT AMINO-ACID SEQUENCE ELONGATION-FACTOR ESCHERICHIA-COLI HA-RAS P21 NUCLEOTIDE-BINDING PROTEIN ROD OUTER SEGMENTS SACCHAROMYCES-CEREVISIAE SIGNAL RECOGNITION PARTICLESJDThe GTPase Superfamily - Conserved Structure and Molecular Mechanism Nature 349 6305117-1273 10 Jan 735 Bourne, H.R. 1991GENE MUTATIONS.'Colon Cancer - Consider the Coiled Coil Nature 351p 6323188-190 16 May 737Bourne, H.R. Stryer, L. 1992~xACTIVATION ADENYLATE-CYCLASE ALPHA CASCADE CYCLIC-GMP PHOSPHODIESTERASE EXPRESSION MECHANISM SUBUNIT TRANSDUCTION VISION,&G-Proteins - The Target Sets the Tempo Nature 358A 6387541-543 13 Aug0)Bourret, R.B. Borkovich, K.A. Simon, M.I. 1991TMSignal Transduction Pathways Involving Protein Phosphorylation in Prokaryotesj$Annual Review of Biochemistry060401-441 738 INCOMPLETE ACCEPTING CHEMOTAXIS PROTEINS BACILLUS-SUBTILIS BACTERIAL ACTIVATOR PROTEIN DIRECTED CROSS-LINKING ESCHERICHIA-COLI K-12 NITROGEN REGULATOR-I SENSORY TRANSDUCTION TRANSCRIPTIONAL ACTIVATOR TUMEFACIENS VIRULENCE GENES VECTORIAL TRANSMEMBRANE RECEPTOR 740 Bowden, G.A. Georgiou, G.` 1990EXPORT GROWTH-HORMONE INCLUSION-BODIES INVITRO INVIVO OUTER-MEMBRANE SECRETION SEQUENCE SOLUBLE RECOMBINANT PROTEINS TRIGGER FACTOR-\VFolding and Aggregation of Beta-Lactamase in the Periplasmic Space of Escherichia-Coli&Journal of Biological Chemistry 26528 16760-16766 5 Oct 741.'Bowden, G.A. Paredes, A.M. Georgiou, G. 1991~ACTIVE-SITE EXPORT GENE GROEL OVERPRODUCING BETA-LACTAMASE RELEASE SECRETION SEQUENCE SOLUBLE RECOMBINANT PROTEINS TEMPERATURENHStructure and Morphology of Protein Inclusion Bodies in Escherichia-Coli98725-730P Aug Biotechnology 739*$Bowden, G.A. Baneyx, F. Georgiou, G. 19922,EXPORTED PROTEINS PERIPLASMIC SPACE SEQUENCEAbnormal Fractionation of beta-Lactamase in Escherichia-Coli - Evidence for an Interaction with the Inner Membrane in the Absence of a Leader PeptideNJournal of BacteriologyI 174T10 3407-3410 May!!/! 7786"Terlesky, K.C. Tabita, F.R.r 1991ATP ESCHERICHIA-COLI FORM-I GENE GROEL PROTEIN LARGE SUBUNITS OXYGENASE PEA-CHLOROPLASTS RHODOPSEUDOMONAS-SPHAEROIDES RIBULOSE BISPHOSPHATE CARBOXYLASEhtnPurification and Characterization of the Chaperonin-10 and Chaperonin-60 Proteins from Rhodobacter-Sphaeroides Biochemistry3033 8181-8186h 20 Aug4.Ternstrm, T. Mayor, U. Akke, M. Oliveberg, M. 1999^From snapshot to movie: f analysis of protein folding transition states taken one step further   VOProceedings of the National Academy of Sciences of the United States of Americab9626 14854-14859:20079571Guanidine Kinetics *Models, Chemical Models, Molecular Mutagenesis Nuclear Magnetic Resonance, Biomolecular Protein Denaturation *Protein Folding Ribonucleoprotein, U1 Small Nuclear/*chemistry/genetics Support, Non-U.S. Gov't ThermodynamicsSJE JAH jchttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.pnas.org/cgi/content/full/96/26/14854e 7788 Terry, M.J. Lagarias, J.C. 19915-AMINOLEVULINIC ACID ALGA CYANIDIUM-CALDARIUM ARABIDOPSIS BILIVERDIN CHROMOPHORE BIOSYNTHESIS GABACULINE INVITRO ISOLATED DEVELOPING CHLOROPLASTS PHYCOCYANOBILIN PISUM SATIVUM LUtilizing an in vitro coupled assay system, we show that isolated plastids from cucumber cotyledons convert the linear tetrapyrrole biliverdin IX-alpha to the free phytochrome chromophore, phytochromobilin, which assembles with oat apophytochrome to yield photoactive holoprotein. The spectral properties of this synthetic phytochrome are indistinguishable from those of the natural photoreceptor. The plastid-dependent biliverdin conversion activity is strongly stimulated by both NADPH and ATP. Substitution of the nonnatural XIII-alpha isomer of biliverdin for the IX-alpha isomer affords a synthetic holophytochrome adduct with blue-shifted difference spectra. These results, together with experiments using boiled plastids, indicate that phytochromobilin synthesis from biliverdin is enzyme-mediated. Experiments where NADPH (and ATP) levels in intact developing chloroplasts are manipulated by feeding the metabolites 3-phosphoglycerate, dihydroxyacetone phosphate, and glucose 6-phosphate or by illumination with white light, support the hypothesis that the enzyme that accomplishes this conversion, phytochromobilin synthase, is plastid-localized. It is therefore likely that all of the enzymes of the phytochrome chromophore biosynthetic pathway reside in the plastid.rXRHolophytochrome Assembly - Coupled Assay for Phytochromobilin Synthase Inorganello&Journal of Biological Chemistryo 266i33 22215-22221 25 Nov 7787xrTerry, C.J. Damas, A.M. Oliveira, P. Saraiva, M.J.M. Alves, I.L. Costa, P.P. Matias, P.M. Sakaki, Y. Blake, C.C.F. 1993AMYLOIDOSIS DISULPHIDE BRIDGE DNA FIBRIL PROTEIN GENE HEREDITARY AMYLOIDOSIS HUMAN PLASMA PREALBUMIN MUTATION POLYNEUROPATHY PREALBUMIN SENILE SYSTEMIC AMYLOIDOSIS THYROXINE-BINDING PREALBUMIN TRANSTHYRETINFamilial amyloidotic polyneuropathy (FAP) is an autosomal dominant hereditary type of lethal amyloidosis involving single (or double) amino acid substitutions in the amyloidogenic protein transthyretin (TTR). The most common type of FAP (Type I, or Portuguese) is characterized by a Val --> Met substitution at position 30. The Met30 variant of TTR has been produced by recombinant methods, crystallized in a form isomorphous with native TTR, subjected to X-rav analysis and compared structurally with the wild-type protein. The comparison shows that the effect of the substitution at position 30 is transmitted through the protein core to Cys10, the only thiol group in the TTR subunit, which becomes slightly more exposed. The variant TTR molecule is otherwise in a near-native state. Use of computer graphics has shown that it is possible to model a linear aggregate of TTR molecules, each linked to the next by a pair of disulphide bonds involving Cys10 residues. Formation of these disulphide bonds involves a small number of slightly short molecular contacts with native TTR molecules, most of which are relieved in the Met30 variant. We propose this model as a possible basis for a molecular description of the FAP amyloid fibrils.TNStructure of Met30 Variant of Transthyretin and Its Amyloidogenic Implications EMBO Journal122n735-741 Feb4635-645 21 Feb 2654*$Godzik, A. Kolinski, A. Skolnick, J. 1992 AZURIN EVOLUTION GLOBIN-PHYCOCYANIN SIMILARITY GLOBULAR PROTEIN HOMOLOGY IDENTIFICATION PLASTOCYANIN PLASTOCYANIN-AZURIN-IMMUNOGLOBULIN SIMILARITY PREDICTION PROTEIN STABILITY PROTEIN STRUCTURE PREDICTION RESOLUTION SEQUENCES SIMULATIONS TIM BARREL SIMILARITYnJDTopology Fingerprint Approach to the Inverse Protein Folding Problem 227y1@227-238 5 Sep"Journal of Molecular Biology&D&2&*2&+2&02&22&42&72&?2&L2&H2&G2&P2(2*2&U2&W2&e2&2&h2&2&v2&s2&z2&2&2&2&2&2'!2'"2'%2+L2+R2+T2+V2)42+Z2+[2+222u22+_2r2+a2'K2)E2+f2f+2f+2+f2+f2+f2+f2+f2+f2+f2+f2+f2+f2+f2+f2us subtilis Ffh, a homologue of mammalian SRP54 protein, that is essential for binding to small cytoplasmic RNA  / &Journal of Biological Chemistry 27122 13140-13146f_Amino Acid Sequence Bacillus subtilis/*METABOLISM Bacterial Proteins/*METABOLISM/GENETICS Base Sequence Molecular Sequence Data Mutagenesis, Site-Directed Peptides/METABOLISM Protein Binding RNA/*METABOLISM RNA-Binding Proteins/*METABOLISM/GENETICS Seque Ottolenghih&nellovosw w wcwbwdw0w1w2w!6w"w2w2w8Rw2'w}winowskiz$ z8 z-] z zelberger+n(u-u+u3u&u&u+u-u-u*u0u1u27u3'u3u4Wu+uRu4a5a#aaabain#dc7~bridge8Hc!chihdega6r7r*r0e0e)0e)/e/e3e7e8le/erfelli4znissi2p/journalsr/ r/ r/ r0 r0 r0 r0 r0 r0 r0 r0 r0 r0 r0 r0 r1 r2 r2 r1> r3 r3 r8! r9r8tt{iCiti i iEiiiXiiMii&i&D3165NS+41S5'7GS7B8s66526N9S672C H7c827c937ACkaaaa!a,a+aCa aeaaaa kaa)hb)b bb#b-[b&bbb"y36'36@36Z33755G37w"bbagh>ora;rowskaC 1CGCCy?hary+dlez-o@o gTe Yelg Zgg.g3nf4af5Zf6f1fforn8s0garagenaisgerAttChBhDhEhGh+hz"qNaturel"u"u# u"u+u#u#u#u*u#u#u*hu$-u$Au$Nu$Tu$ju$mu$u$u$u$u$u%Uu%du%~u%u%u%u&Ru*u&u)u+Qu+Tu+cuuHu+wu+u+u'u&u(u(u(u(u(u(u(u(u(u(u(u(u(u(u(u(u(u(u(u 1993,%AAC2 ADENINE-NUCLEOTIDE TRANSLOCATOR ADP ATP TRANSLOCATOR ADP-ATP CARRIER AMINO-ACID SEQUENCE BEEF-HEART MITOCHONDRIA BROWN ADIPOSE-TISSUE ESCHERICHIA-COLI FAT UNCOUPLING PROTEIN MESSENGER-RNA PROTEIN ENGINEERING SACCHAROMYCES-CEREVISIAE SITE-DIRECTED MUTAGENESIS STRUCTURAL RELATIONSHIP YEASTztSite-Directed Mutagenesis of the Yeast Mitochondrial ADP/ATP Translocator - 6 Arginines and One Lysine Are Essential 2304 1159-1170 20 Apr"Journal of Molecular Biology FEDC)B@JA>|? 4915,&Matsuyama, S. Kimura, E. Mizushima, S. 199082ATP ATPASE BINDING PROTEIN SECA SITE TRANSLOCATINGvoSecA is a protein translocation ATPase. The secA gene was engineered so as to code for SecA fragments of different sizes, either from the amino terminus or the carboxyl terminus. These SecA fragments, most of which formed aggregates in the cytosol, were overproduced and then purified in the presence of 6M guanidine hydrochloride. The fragments were renatured by means of diln. and dialysis, and then examd. as to their ability to interact with ATP by means of photoaffinity crosslinking with [.alpha.-32P]ATP. Individual SecA fragments thus renatured were inactive as to ATP binding. However, when 2 fragments (amino- and carboxyl-terminal ones), which structurally complemented each other and which had an overlapping region, were mixed, crosslinking was obsd. at the amino-terminal segments. The crosslinking was appreciably enhanced when 2 such fragments were first mixed together in 6M guanidine hydrochloride and then renatured. It is concluded that SecA has an ATP-binding domain near its amino-terminal region and that the binding requires a carboxyl-terminal fragment that is large enough to cover the region deleted from the amino-terminal fragment. An amino-terminal fragment, which constituted about 92% of the entire SecA mol., was active in not only ATP binding but also protein translocation. Based on these findings, the structure-function relationship of SecA is discussed.  0021-9258iComplementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region&Journal of Biological ChemistryS 26515 8760-8765Tokyo 113, Japan.'Matsuyama, S. Akimaru, J. Mizushima, S.a 1990SecE-Dependent Overproduction of Secy in Escherichia-Coli - Evidence for Interaction Between 2 Components of the Secretory Machinery FEBS Letters 269 1e 96-100 20 Aug 4911rlCONSTRUCTION EXPRESSION GENE INSERTION MEMBRANE-PROTEINS MUTANT MUTATION PROTEIN EXPORT SYSTEM TRANSLOCATION 491481Matsuyama, S. Fujita, Y. Sagara, K. Mizushima, S.  1992ATP EXPORT PHOSPHOLIPIDS PRESECRETORY PROTEINS PROTEIN SECRETION PROTON MOTIVE FORCE RECONSTITUTION REGION SECD SECF SECRETION MACHINERY SECRETORY MACHINERY SIGNAL PEPTIDE VESICLESOverproduction, Purification and Characterization of SecD and SecF, Integral Membrane Components of the Protein Translocation Machinery of Escherichia-colii$Biochimica et Biophysica Acta 11221 77-84 13 Jul 4912,&Matsuyama, S. Fujita, Y. Mizushima, S. 1992NGCDNA CLONES EXPORT EXPRESSION GENE-PRODUCT IDENTIFICATION TRANSLOCATIONI`YLarge-Scale Production of Membrane Proteins Fused to a Truncated Seca in Escherichia colic0)Bioscience Biotechnology and Biochemistryn569e 1512-1514t Sep 4913,&Matsuyama, S. Fujita, Y. Mizushima, S. 1993ANTI-SECD IGG ATP ESCHERICHIA-COLI EXPORTED PROTEINS GENE MALTOSE BINDING PROTEIN MUTATIONS OUTER-MEMBRANE PRESECRETORY PROTEINS PROTEIN RELEASE PROTEIN SECRETION RECONSTITUTION SECD PROTEIN SIGNAL-SEQUENCE VESICLESaztSecD Is Involved in the Release of Translocated Secretory Proteins from the Cytoplasmic Membrane of Escherichia-Coli EMBO Journal121265-270 Jan2*#Matsuyama, S. Tajima, T. Tokuda, H. 1995A novel periplasmic carrier protein involved in the sorting and transport of Escherichia coli lipoproteins destined for the outer membrane EMBO Journal1414 3365-3372 4916 Mattaj, I.W. 1993("BINDING MOTIF PEPTIDES REVEALS TAT(!RNA Recognition - A Family Matter  Cell735837-840 4 Jun 4917*#Matter, K. Hunziker, W. Mellman, I., 1992CANINE KIDNEY-CELLS DENSITY LIPOPROTEIN RECEPTOR ENDOPLASMIC-RETICULUM INFLUENZA-VIRUS HEMAGGLUTININ INTRACELLULAR-TRANSPORT LYMPHOCYTE FC-RECEPTORS MEDIATED ENDOCYTOSIS PLASMA-MEMBRANE PROTEINS POLYMERIC IMMUNOGLOBULIN RECEPTOR TRANSMEMBRANE PROTEINST~Basolateral Sorting of LDL Receptor in MDCK Cells -The Cytoplasmic Domain Contains 2 Tyrosine-Dependent Targeting Determinants Cell715741-753 27 Nov Matthew, J.B. Gurd, F.R.N. 1986<6Calculation of electrostatic interactions in proteins. 130413-436 Methods in Enzymology  4930PJMatthews, C.R. Crisanti, M.M. Gepner, G.L. Velicelebi, G. Sturtevant, J.M. 1980AMINO ACIDS. CALORIMETRY, DIFFERENTIAL SCANNING. DRUG STABILITY ESCHERICHIA COLI/EN [ENZYMOLOGY]. HEAT. PROTEIN DENATURATION. SUPPORT #TRYPTOPHAN SYNTHASE U.S. GOV'T, NON-P.H.S. SUPPORT, U.S. GOV'T, P.H.S. THERMODYNAMICStnEffect of single amino acid substitutions on the thermal stability of the alpha subunit of tryptophan synthase Biochemistry197y 1290-1293y 1 Apr SJE. Z/@"4Devos, D. Valencia, A. 2000.'Practical limits of function predictione2+Proteins: Structure, Function, and Geneticsi41 98-107 KSR 1700Dewit, T.F.R. Bekelie, S. Osland, A. Miko, T.L. Hermans, P.W.M. Vansoolingen, D. Drijfhout, J.W. Schoningh, R. Janson, A.A.M. Thole, J.E.R.e 199265-KILODALTON ANTIGEN BOVIS BCG COMMON ANTIGEN ESCHERICHIA-COLI HEAT-SHOCK OPERON LEPROSY PATIENTS MOLECULAR-CLONING NUCLEOTIDE-SEQUENCE PROTEIN TUBERCULOSISEIn contrast to other bacterial species, mycobacteria were thus far considered to contain groEL and groES genes that are present on separate loci on their chromosomes, Here, by screening a Mycobacterium leprae lambda gt11 expression library with serum from an Ethiopian lepromatous leprosy patient, two DNA clones were isolated that contain a groEL gene arranged in an operon with a groES gene. The complete DNA sequence of this groESL operon was determined. The predicted amino acid sequences of the GroES and GroEL proteins encoded by this operon are 85-90% and 59-61% homologous to the sequences from previously characterized mycobacterial GroES and GroEL proteins. Southern blotting analyses with M. leprae groES- and groEL-specific probes demonstrate that similar groESL homologous DNA is present in the genomes of other mycobacteria, including Mycobacterium tuberculosis. This strongly suggests that mycobacteria contain a groESL operon in addition to a separately arranged second groEL gene. Using five T-cell clones from two leprosy patients as probes, expression of the M. leprae GroES protein in Escherichia coli after heat shock was demonstrated. Four of these clones recognized the same M. leprae-specific GroES-derived peptide in a DR2-restricted fashion. No expression of the groEL gene from this operon was detected in E. coli after heat shock, as tested with a panel of T-cell clones and monoclonal antibodies reactive to previously described GroEL proteins of mycobacteria.MvpMycobacteria Contain 2 groEL Genes - The 2nd Mycobacterium-Leprae groEL Gene Is Arranged in an Operon with groESMolecular Microbiology614 1995-20078 Jul 1701XQDewolf, F.A. Maliepaard, M. Vandorsten, F. Berghuis, I. Nicolay, K. Dekruijff, B.o 1990CONTAINING MODEL MEMBRANES EQUILIBRIUM-BINDING HUMAN-ERYTHROCYTES NATURAL MEMBRANES NEGATIVELY CHARGED PHOSPHOLIPIDS NUCLEAR MAGNETIC-RESONANCE PROTEIN KINASE-C RAT-HEART SELF-ASSOCIATION UNILAMELLAR PHOSPHATIDYLCHOLINE VESICLES|vComparable Interaction of Doxorubicin with Various Acidic Phospholipids Results in Changes of Lipid Order and Dynamics$Biochimica et Biophysica Actah 10961 67-80e 14 Nov 1702,&Dewolf, F.A. Nicolay, K. Dekruijff, B. 1992ACIDIC PHOSPHOLIPIDS ANTHRACYCLINE DERIVATIVES APOCYTOCHROME-C CYTO-TOXICITY HEXAGONAL PHASE-TRANSITION MITOCHONDRIAL-MEMBRANES NEGATIVELY CHARGED PHOSPHOLIPIDS NEURO-BLASTOMA CELLS NUCLEAR MAGNETIC-RESONANCE PROTEIN KINASE-CEffect of Doxorubicin on the Order of the Acyl Chains of Anionic and Zwitterionic Phospholipids in Liquid-Crystalline Mixed Model Membranes - Absence of Drug-Induced Segregation of Lipids into Extended Domainsa Biochemistry3138 9252-9262 29 Sep:4Dhanasekaran, M. Fabiola, F. Pattabhi, V. Durani, S. 1999.(A rationally designed turn-helix peptide J.Am.Chem.Soc 121  5575-5576|peptide desin, NMR 1704 Dhingra, M.M.\ 1992ARG GLY ASP ECHISTATIN FIBRONECTIN FRAGMENTS MAGNETIC-RESONANCE PEPTIDES PROTEINS RECOGNITION SITE SECONDARY STRUCTURE SPECTROSCOPYFJDSolution Conformation of a Model Hexapeptide Containing RGD Sequence296y458-464i Dec4-Indian Journal of Biochemistry and Biophysics 1719*#Di Cera, E. Robert, C.H. Gill, S.J. 1987\VAllosteric interpretation of the oxygen-binding reaction of human hemoglobin tetramers Biochemistry2613 4003-4008r 30 Jun 171381Di Cera, E. Doyle, M.L. Connelly, P.R. Gill, S.J.  19874.Carbon monoxide binding to human hemoglobin A0 Biochemistry2620 6494-6502 6 Oct  1718& Di Cera, E. Gill, S.J. Wyman, J. 19886/Canonical formulation of linkage thermodynamicsa8514 5077-5081 JulVOProceedings of the National Academy of Sciences of the United States of AmericaF 1717& Di Cera, E. Gill, S.J. Wyman, J. 1988B7ESCHERICHIA MUTATION PLEIOTROPIC PROTEIN SECA SECRETIONPleiotropic mutants of E. coli defective in protein secretion were isolated using a strain carrying a fusion between the malE gene and the lacZ gene. This strain produces a hybrid protein, with the N-terminus being derived from the periplasmic maltose-binding protein (MBP) and the C-terminus from the cytoplasmic enzyme .beta.-galactosidase. The cytoplasmic location of the hybrid protein facilitates the selection of secretion-defective mutants. One important feature of this system is the sensitivity to slight changes in the secretory ability of the cells. The secretion of MBP at 30.degree. in both secA and secB mutants was .gtoreq.90% of the wild-type. However, after exposure to heat (37.degree. or 42.degree.) for 2 h, the mutants became almost totally defective in MBP secretion. 0300-5410PIPleiotropic mutants affecting the secretory apparatus of Escherichia coli 133A1105-110Boston, MA 02115, USA-$Annals of Microbiology (Paris) Oliver, D. 1985,%Protein secretion in Escherichia coli$Annual Review of Microbiology39,615-48  Stony Brook, NY 11794, USA 57140)ESCHERICHIA PROTEIN REVIEW SECA SECRETIONA review with 195 refs.d 0066-42271^HTtp01_u1`u1au1bu1cu1du1eu1fu1gu1hu1iu1ku1lu1mu1nu1ou1pu1qu1ru1su1tu1uu1vu1wu1xu1yu1zu1{u1|u1}u1~u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1u1NIH1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1e1Ofc1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1NNNN1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N1N.N1N1N1N1N1N1N1Ngments of a staphylococcal nucleaseo584d 1806-1811 Oct VOProceedings of the National Academy of Sciences of the United States of AmericaP 164Anfinsen, C.B. 1967:3The formation of the tertiary structure of proteinsLHarvey LecturesE61 95-116 165Anfinsen, C.B. 1968f_Characterization of staphylococcal nuclease and the status of studies on its chemical synthesis173461-517 Pure and Applied Chemistryf,POWer2f"f#f6f7fvful s*xs3Ms7Ksss!s5s6s6&s6(s7s7Hs7Is7s7s8s8s8)s88s8<s8Ms8ings }Piiiiiii)i*5i)$i#i$wi+ci+di+i6Ji7ioislrlllsn'nallxton5yart53@ zdnyakovananskiPoP56<1116A1>125 60sC/c&zc p5s6s&6s(6s7sH7ss} Piiiiiii)i5*i$)i#iw$ic+id+i+iJ6i7ioislrlllsn'nallxton5yart5@3 zdnyakovananskiPoP56<111A61>125 60sC/cz&c p ThIOcyanate S$Pester6 A7 A7 A7 A7 A ASE7 s8  f8  f8  f7 f8flavine es GALACTOSIDELUCOSIDES% YsYCOSIDESl lsss$s+Qs3Ns6ssps A A AAwAQARAAAAaaaa$Pa,a!a6aases s!*sslst t!*t#t#t'tes)<sm 'mm1UU$eU UBTILISIN methylene%nen insu O) ucleotidesr hr$ phosphateredoxin    y       '  I 7 S H E p   ar  $K %y %x + -> m- e1 n4 A A A I 7 S H E pA A  T DIfferent f  * ` l  s p 2 e * . 2 B    >     z 1 ~    L ] h       ![ " "v # #M # $ $ $ % % % & + ( ,[ ,  -T - - - - - * . #x / 0  0S . &] [ 10 1@ 1 1 1 2 2 3 37 3 5 6s 6 3 g #^ $  A   *   L ] h        ![ " "v # #M #x # $ $ $ % % % &] 3 A g  #^ $  MLRapoport1990 jRapoport1991Rapoport1991Rapoport1991'Rapoport1992'Rapoport1992Rapoport1992Rapoport1992fRapoport1992 Rapoport1992 kRapoport1993 lRapoport19933'Rapoport1993Rapoport19939 Rapoport1993Rapoport19949Rapoport19959Rapoport1995 iRapoport19962Rapoport199697]Rapoport19969+hRapoport19979+8Rapoport19988*Rapoport1998)#Rapoport19989+KRapoport19989,~Rapoport199890iRapoport199991vRapoport19991wRapoport199991xRapoport199991sRapoport200001tRapoport20001uRapoport20000Rapoport200111^Rapoport20012Rapoport2001D3Rapoport200103Rapoport2002|4%Rapoport20024~Rapoport2002o8ERapoport2003e8Rapoport200448Rapoport200445 Raposo2003 Rapoza1993  Rapp1993v, Rappe1998Rappuoli19922Rappuoli1993*s Raquet19966 Rarick19939* Rarick19979/ Raschke1997. Raschke19992M Raschke1999Rasenick1990$Rasenick1991#Rasenick1991Rasenick19931 Rasheed1990 Rasheed1992T Rashin19755 Rashin1984  Rashin1985  Rashin1986 Rashin1993 ! Rask19851! Rask19851 Rasmussen1985 Rasmussen1987 Rasmussen1991# Rasmussen19932 Rasmussen2002L Rasool1993 $ Rassart1993#pRassoulzadegan1992 Rassow1990 & Rassow1991  Rassow1991  Rassow19922x Rassow19922 Rassow1992 c Rassow1992  Rassow1993  Rassow199332 Rassow200001C Rassow200102 Ratajczak1999? Ratanavanich19934 Ratcliffe1992 Rath1991v Rath19933 Rath1993v* Rathgeb-Szabo1998*j Rathgeb-Szabo1998 Rathinavelu1993/o Ratliff19992 Ratliff2002 Ratna1991( Ratnaswamy1997  Ratner19891 Ratner1991  Ratner19939 Ratner19933- Ratner199916l Ratner19990 Ratner2000&Y Rau1991&Y Rau1991 Rau1992* Rau199849 Rauch20027' Rauch20025 Rauch2003 Rauchberger1979| Raugei19933+ Raugei19981Raulston19932Raulston20011 Raushel19905 Raushel1993 Raushel1993*r Raushel1996 ~ Raushel1996( Raushel199766Raussens19991% Rauzier1991Ravagnan19911 Ravazzola1991 Ravazzola1993 Ravazzola1993! Ravazzola1993 Ravazzola1993& Ravichandran1995Ravindra1990#} Ravishanker1993 Ray1990 Ray1992 Ray1993. Ray1999 Rayburn1995 Raychaudhuri1992. Rayment1993 Rayment19937 Rayment1996" Raymer19931#A Raymond19924 Raymond2002 Rayner1991 5 Raynes20030 Raynor1991  Raynor1993 / Raza19979 Razgulyaev1989 ^ Razgulyaev1990  Razgulyaev1991  Razgulyaev1991 0?Razzaque19980 Reader2000, Reagan1998 Reardon1989 Reardon1992 Reardon19932O Reardon1999 Reason19933 Reay1993w Reay19939 Rebay1993  Reboud1993  Reboud19933+ Reboud19939 Reboudravaux1990.Receveur19983/pReceveur1999.C Recio1999 Recny1993+ Recny1993+ Recny1993 A Record1989 F Record1989  Record1991 G Record1992 I Record1994 5l Record20030 Reddehase1991 Reddehase1992 Redding1991$ Redding1992$? Reddy1990z Reddy1990 X Reddy1992 Reddy1992 Reddy1993 Reddy1993 Reddy1993 Reddy1993? Reddy1993? Reddy1993$ Reddy1994#U Reddy1996/f Reddy19996t Reddy199938 Reddy2002 Redeker1991Y Redelmeier1993  Redfern1993 RRedfield1985"Redfield1985!Redfield1985Redfield1985+Redfield1987Redfield1988Redfield1990Redfield1990Redfield1991Redfield1991Redfield19919Redfield1991Redfield1991Redfield19911Redfield19925Redfield19929Redfield1992Redfield19933Redfield19931Redfield1993Redfield1994'CRedfield1995]Redfield1995(Redfield1997(Redfield1997-Redfield19999.9Redfield1999.Redfield199936Redfield199993,Redfield2002w3IRedfield200225Redfield20030 Redhardt19922  Redlinski1992 Redmer1993a  Redziniak1990 Reece1989*h Reece1997 Reed1990v#y Reed19909 Reed1991v v Reed1991t,M Reed1991 Reed19929 Reed1992v Reed19929 s Reed1992i,N Reed1994,P Reed199592 Reed19959,O Reed19969*A Reed19971*f Reed1997v,Q Reed19977, Reed199812 Reed199912 Reed2000217 Reed200102 Reed200108 Reed200123 Reed20020 Reedijk1992) Reedijk19964 Rees1983 Rees1990v Rees1990v Rees19919 Rees19919~ Rees199194 Rees1992 Rees1992y Rees19921 Rees19939# Rees1993v Rees19931) Rees19976 Rees19976 Rees19989 Reese19923 Reese1992 Reese19938+ Reese2003# Reeve1991,( Reeve1998 Regan1993 Regan1993* Regan1994 Regan1995 Regan1996( Regan1997/~ Regan19977+ Regan1997, Regan1998, Regan19992 Regan19996 Regan20015] Regan20038 Regan2003G Regazzi1993A Regenstein1975  Reggelin1992  Regier1993 ` Reginelli1992  Regis1993  Regland19920_ Regnacq1997  Rehaber1990 Rehaber1991 Rehaber19938a Rehbein20038` Rehling20034 Rehman1992  Reich1992 Reich1993 Reich1994)Reichert19929 Reichert1993Reichlin1992 Reichmuth1993 Reid1991v" Reid19919~ Reid19921 Reid19929" Reid19929 Reid19931 Reid199319931 Reid19931Redfield19919Redfield1991Redfield1991Redfield19911Redfield19925Redfield19929Redfield1992Redfield19933Redfield19931Redfield1993Redfield1994'CRedfield1995]Redfield1995(Redfield1997(Redfield1997 Redhardt19922  Redlinski1992 Redmer1993a Reece1989*h Reece1997 Reed1990v#y Reed19909 Reed1991v v Reed1991t Reed19929 Reed1992v Reed19929*A Reed19971*f Reed1997v Reedijk1992) Reedijk1996 Rees1990v Rees1990v Rees19919 Rees19919~ Rees199194 Rees1992 Rees1992 Rees19939# Rees1993v Rees19931 Reese19923 Reese1992 Regan1993 Regan1993* Regan1994 Regan1995 Regan1996G Regazzi1993A Regenstein1975  Reggelin1992  Regier1993 ` Reginelli1992  Regis1993  Regland1992  Rehaber1990 Rehaber1991 Rehaber19934 Rehman1992  Reich1992 Reich1993 Reich1994)Reichert19929 Reichert1993 Reichmuth1993 Reid1991v" Reid19919~ Reid19921 Reid19929" Reid19929 Reid19931 Reid19931 Reid19931Reid19931<)immunodeficiency!o%P%P)P6P6P6P7dP8]P$)PLETION0tection,N ificiencyominant Dedee)ee%eSee9electronF FF FFF ,F%N$ NZYMOMETRIC FLUORESCENCEG g g g'gg&0g)gen E ETICs  sIi icI I I I" I I I I I% I I Iu I  i * i i i330 1 d1 ,111(111&1141 1!1+1O1.C11P111 900 0 0$O05050606080 0$07/1 1 123.467/89X91F13^3:33 33e33u3" 3"R3#j3$3&3.E3.303537U3i3':3 A26[00+X05050608G08I08J000$01cewonger, R. B.; Begley, T. P.; McLafferty, F. W. J. Biol. Chem. 1997, 272, 32215-32220. (31) Miranker, A. D.; Kruppa, G. H.; Robinson, C. V.; Aplin, R. T.; Dobson, C. M. J. Am.,G2!9222 U22#22n2q2p2M2(2 2 222p2q222*2)2,2+2-2/2{2}2 C2!<2!;2!:2$G2$2$2%l2%k2-32-72-:2,2-F2-G2-M2-R2,2,2-V2-W2-[2-_2-f2-k2h2-m2-r2-2-2-2-2-2-2```aaaaaacccccccccaaaaaa``````aaaaaa```aaaaaaaaaccc``````aaaaaaaaaaaaaaaaaa````````````aaaaaa``````]]]]]]]]]]]]cccLLL444111***************)))&&&)))***---LLLfffSSS***---333333999MMM[[[kkkzzzjjj666hhheCationsusedgmvanagh++ ityCP+DkC2N=NAl Meells)s*s s kssssFsuss#s)css $ssGss(<s s#sLs!rrr wu uuuuu9uu+uularslss sJsennterl)v's"'s `ral%'esvrai-Evisiae H  H t tEtainH gFTRGid"H#H#H%RPd& Hadwicke inZsusopyright restrictions and are referred to the publication data appearing in the bibliographic citations, as well as to the copyright notices appearing in the original publications, all of which are hereby incorporated by reference. Users should consult legal counsel before using NLM-produced records to be certain that their plans are in compliance with appropriate laws. Disclaime2&NIH2+e/e2-e2.e/e21e/e/e22e23e24e25e26e27e28e29e2:e2;e2<e2=e2>e2?e2Be2@e2Ce2De2Ee2Ie2He2Ge2Fe2Je2Ke2Ne2Me2Le2Pe2Qe2Re2Te2Se2Ve/e2Xe2Ze2Ye2[e2\e2]e2_e2^e2`e2ae2be2de2ce2ee2fe2fe2fe2fe2fe2felakis*[AUTH]+AND+muirphy*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Connecting to host... Connecting to host... Searching for: [kanelakis*[AUTH]+AND+murphy*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host.*1RSsa211711311D7p1p2D6pDDEGH6Zmplesb tDS18S3S S"C1c16E#G0aI1 I1I I&]I1 I0`II/9I)0I)/I/I"I1I1III1I0I1'II.I*II&II0I);I)[I0I0JI"II):I)?I@I=I2I0I0I1 ISI0Ienkov19981 Slepenkov19981O Slepenkov2001 Slepushkin1993  Slice1990 Sligar1991r  Sligar1991  Sligar19939- Sligar199336 Sligar19933  Sligar1994 ~ Slim1993Slingsby1993* Sliwkowski19988 Sloan1993Slomiany1992Slomiany19929Slomiany19929 Slonim1992s Slonim1992  Slonim19939 Slonim19939. Slonimski1993 2  Weisgraber$ l$ l$Vleder$W s4sb b b b3b4b5b6bfbb3b4bbb<bbbbbCb)b"Ab$Xb$[b$Zb$Yb$^b$]b$\b$_b$`b$ab+PbNb-b/>b0b,b4b5ab6"b6Db6b6b=bachE E EENBERGh$ h,}hornzhart$b ooff4ign#man$cn$hn$gn$fnto server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 4 - 6... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Done retrieving references Done Connecting to host... Connecting to host... Searching for: [king*[AUTH]+AND*Low&e ert&btdcucchesi\gerQMINALnneyt"thert+{ yCOPERSICON mphOcytesHma#siney` OLECITHIN6zymeMeMMM#M sMMMMPaaaQaaaOaaaZaaa ~a a ca a /a a a <a a a =a a aXaaEa11x11$111S111 |{z.y>vw^x"utf 1798"Donnelly, C.E. Walker, G.C.r 1992BACTERIOPHAGE MORPHOGENESIS CLEAVAGE ESCHERICHIA-COLI GENE IDENTIFICATION MITOCHONDRIA MUTATIONS OVERPRODUCTION RECA PROTEIN SOS MUTAGENESISThe GroE proteins of Escherichia coli are heat shock proteins which have also been shown to be molecular chaperone proteins. Our previous work has shown that the GroE proteins of E. coli are required for UV mutagenesis. This process requires the umuDC genes which are regulated by the SOS regulon. As part of the UV mutagenesis pathway, the product of the umuD gene, UmuD, is posttranslationally cleaved to yield the active form, UmuD'. In order to investigate what role the groE gene products play in UV mutagenesis, we measured UV mutagenesis in groE+ and groE strains which were expressing either the umuDC or umuD'C genes. We found that expression of umuD' instead of umuD will suppress the nonmutability conferred by the groE mutations. However, cleavage of UmuD to UmuD' is unaffected by mutations at the groE locus. Instead we found that the presence of UmuD' increased the stability of UmuC in groE strains. In addition, we obtained evidence which indicates that GroEL interacts directly with UmuC.^XCoexpression of UmuD' with UmuC Suppresses the UV Mutagenesis Deficiency of groE MutantsJournal of Bacteriologyn 174 10 3133-3139 Maye 1799 Donnelly, D. 1993lfHYDROPHOBICITY MEMBRANE-PROTEINS PHOTOSYNTHETIC REACTION CENTER PROTEIN STRUCTURES RESOLUTION SEQUENCE4-Modelling alpha-Helical Transmembrane DomainsE& Biochemical Society Transactions211  36-39e Feb 1802Donnelly, J.J. Ulmer, J.B. Hawe, L.A. Friedman, A. Shi, X.P. Leander, K.R. Shiver, J.W. Oliff, A.I. Martinez, D. Montgomery, D. Liu, M.A. 1993~wCELLS CYTOSOL DIPHTHERIA-TOXIN DOMAIN ESCHERICHIA-COLI INFLUENZA NUCLEOPROTEIN PROTEINS RECOGNITION TOXIC LYMPHOCYTES-TO|vTargeted Delivery of Peptide Epitopes to Class-I Major Histocompatibility Molecules by a Modified Pseudomonas Exotoxin908` 3530-3534P 15 AprVOProceedings of the National Academy of Sciences of the United States of America 1801NHDonnelly, D. Overington, J.P. Ruffle, S.V. Nugent, J.H.A. Blundell, T.L. 1993@:3-DIMENSIONAL STRUCTURE 3A RESOLUTION BACTERIORHODOPSIN FOURIER TRANSFORM HYDROPHOBICITY LIPID-ACCESSIBLE SIDE CHAINS MEMBRANE-PROTEINS PERIODICITY PHOTOSYNTHETIC REACTION CENTER RHODOBACTER-SPHAEROIDES R-26 RHODOPSEUDOMONAS-VIRIDIS SECONDARY STRUCTURE PREDICTION SEQUENCE SUBSTITUTION TABLES TRANSMEMBRANE HELICES~wModeling alpha-Helical Transmembrane Domains - The Calculation and Use of Substitution Tables for Lipid-Facing Residues3Protein Scienceg2e1 55-70c Jan 1800 Donnelly, D. Cogdell, R.J. 1993ANTENNA COMPLEX FOURIER TRANSFORM HYDROPHOBICITY MEMBRANE-PROTEIN MEMBRANE-PROTEINS MOMENT ORGANIZATION PROTEIN MODELLING SECONDARY STRUCTURE PREDICTION SEQUENCE SPHAEROIDES TEMPLATESrPredicting the Point at Which Transmembrane Helices Protrude from the Bilayer - A Model of the Antenna Complexes from Photosynthetic BacteriaeProtein Engineeringl6r6629-635c Aug2 1803(!Donnellyroberts, D.L. Lentz, T.L.R 1993&ACETYLCHOLINE RECEPTOR ALPHA-BUNGAROTOXIN BUNGAROTOXIN BINDING-SITE CARBAMYLCHOLINE CIRCULAR-DICHROISM CONFORMATION CONFORMATIONAL STATES GEL-ELECTROPHORESIS HIGH-AFFINITY BINDING LIGAND MARMORATA PROTEIN PURIFIED ALPHA-SUBUNIT RESIDUES 173-204 SODIUM DODECYL-SULFATE TORPEDO-CALIFORNICASodium Dodecyl Sulfate-Induced and Carbamylcholine-Induced Changes in Circular Dichroism Spectra of Acetylcholine Receptor Synthetic PeptidesMolecular Brain Research19 1-2 55-61 Jul 1805.'Donovan, J.M. Jackson, A.A. Carey, M.C. 1993ACIDS BILIARY LIPIDS CHOLESTEROL CHOLESTEROL MONOHYDRATE CRITICAL MICELLAR CONCENTRATION GALLSTONE DISSOLUTION HYDROPHOBICITY MICELLES PHASE PHYSICAL-CHEMICAL BASIS TAUROCHENODEOXYCHOLATE-LECITHIN TAUROCHOLATE-LECITHIN URSODEOXYCHOLATE PROTECT VESICLESMolecular Species Composition of Inter-Mixed Micellar/Vesicular Bile Salt Concentrations in Model Bile - Dependence upon Hydrophilic-Hydrophobic Balance Journal of Lipid Researchs347m 1131-1140B Jul. 1806 1972 INCOMPLETEHelvetica Chimica Acta55947-9616/Donzel, B. Kamber, B. Wthrich, K. Schwyzer, R. Doolittle, R. 1989(!Redundancies in protein sequences  Fasman, G.D.PJPrediction of Protein Structure and the Principles of Protein Conformation  New York, NY  Plenum Press599-623  1807AK`6t!z!z,6$$+=`-wGGq'U--$-dw2-xv!-+wQy$iYA- $*ss66w&$"(<J!){Z(-){%#*Y z&&e(& K>9+ X,)k !F:!m$;&-&-m#%m *h$-'U,% <#d(,Z DP[rG[!(n,nQ/1&"Rw+i$S) iE },"A&v+4&-!1KM1L11M11N11O11P11Q11R11S11T11U11W11X11Y11Z11[11\11]11^11_11`11a11b11c11d11e11f11g11h11i11k11l11m11n11o11p11q11r11s11t11u11v11w11x11y11z11{11|11}11~111111111111111111111111111116... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Done retrieving references Done Connecting to host... Connecting to host... Searching for: [Shortle+D*[AUTH]+AND+NMR[ALL]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... C.% BIOchemical%  s%= s%C s%G s%P s%S s%R s%T s%` s% s% s+ s&4 s&M s& s& s'# s& s'M sW s s" s, s s* s%i s- s- s.L s.^ s._ s/) s/< s/E s) st sM s( s07 s08 s0B s0I s0H s0 s1$ s s0 s.K s.J s/  s3 s4 s4 s4 s5 s s $ s  s s s s s s s!a s# s  sz/query?db=m&form=6&dopt=r&uid=8117701JDBagby, S. Harvey, T. S. Kay, L. E. Eagle, S. G. Inouye, S. Ikura, M.Unusual helix-containing greek keys in development-specific Ca(2+)- binding protein S. 1H, 15N, and 13C assignments and secondary structure determined with the use of multidimensional double and triple resonance heteronuclear NMR spectroscopy'^XDivision of Molecular and Structural Biology, Ontario Cancer Institute, Toronto, Canada.8117708CHEmA8i8i8i8i8i8+i80i82i8<i8=i8>i8Ki8Mi8Oi8Ui8[i8_i8ai8ci8gi8hi8ji8li8mi8ni8oi8pi8qi8ti8wi8|i8}i8~i8i8i8i8i8i8i8i8i8i8i8i8i8i8i9 i9Mi9Vi9Yi9[i9\i9]i9_i9ei9fi9Xi9ji9ki?i7i ee8i8i8i8i8+i80i82i8<i8=i8>i8Ki8Mi8Oi8Ui8[i8_i8ai8ci8gi8hi8ji8li8mi8ni8oi8pi8qi8ti8wi8|i8}i8~i8i8i8i8i8i8i8i8i8i8i8i8i8i8i9 i9Mi9Vi9Yi9[i9\i9]i9_i9ei9fi9Xi9hi?i7i ee1WWW1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y1y endoplasmic r r% r{ r r r r  r  r . r  r  r  r  r  r  r!  r!  r!# r!4 r!7 r!l r! r! r! r" r"6 r"A r#? r#g r#o r#t r# r$ r$- r$j r$p r$ r$ r$ r%+ r%L r%M r%e r%f r% r% r% r% r&M r& r' r)) r+X r+Z r+c r r r+h r r+i r+j r4PRoteinU(4&*444 &44$'Z% %Q4%j%D$/54+<25 5(525456/5<5;5=5>5C5H5K5L5R5U5Y5X5V5]5\5d5c5`5l5i5m5q5o5o5oCHEMICALll/lcl=l^llKllll l l!Jl!l"l#Ml#l#l$l$l$l% l%Nl%sl%l%l&Al&Jl&l+qlll,l-l%l,l!:ll/l/l/l/l/l/l/l#'l#$l#%l/l/l4l4l*l% l6l6 l6#l6+l6.l68l6Gl6Rl6el6wl6l6l6l6l6l6l7l7l7l7+l7<l7Al7Il7hl7ml7ql7l7l7l7l7l7l7l7l7l7l7l7l7l7l7l7l7l8l8)l8[l8pl8l8l8l8ll)lll)l6l6l6leAutoregulatory"pressioni$s!somalC timulationT7 transporter7s XIDATIONV  VE*Lx66'i3iliaryn1;nn en%oo eoS%S eSotrophy v1e'V0 ailabilityl) l l+ l7 l7 l8! l8 l6lebC b - b< b+  b~ b  b" b+^ b+p b'S b5 n6! n6# n6} n6 n7f n7 n7 n7 n8 n8! n8F n8f n8m n8 n8 n8 n46'ncats3esyanbelj*e- e5d8d4deeva4e7e1'eknn!nnarrrrrLow'0ppUpp p Ap p p ppZpYp^ppppppppppppp'ppppppfp!pp |p p p p p!p!p"p#p$ p$1p$p$ppppe e e e e jeeeeexeye]e These!ft!t!t!t"4t"ut"vt"xt"yt"t)t#/t#0t#^t#zt#{t#t#t#t$&t$Ut%'t%t&t&/t&0t&Ot&_t&t)%t)&t)'t)(t),t)-t))t+Zt+[t+\t%t+et+gt+ht+it+jt+lt&t+ot+qt'Ptot+wt+yt+}tOtt,t,t-t'Stst+tt" \}{W%q)|q+K#_-,H+ *X/,&O-jv=-{sc| )FoK)$&-o+$ o+);$S+)k-))*&v-oV&(x5#$")Uy -$$h+v) 5(mC%~ +x&# &{-{iooI$@2-g|$*g*>"w56]'p0"G!yX\5w,g()$;'OO>'O-o](skq_$XR( +p 1p(x!|8} Breuker2002hBreukink1992gBreukink1992#Breukink19931jBreukink1993iBreukink1993kBreukink1994 Breukink1994lBreukink1995#+Breukink19969)XBreukink19971n Brew1970v v Brew1975v Brew19844 Brew1989v& Brew1996d- Brew199996 Brew199993m Brew200104i Breward2003 Brewer1992 3S Brewer1999< Breyer1984p Breyer1989 o Breyer1989  Breyer1991s0 Breyton20014% Breyton20029 Brian2004 Briancon199330\ Briand19971- Brice1977 : Brick19850M Brickenden1993% Bricker1992Brickman1978qBrickman1984,Brickman1990 Brickmann1991cBricogne1982) Bridger1991 Bridger1992 Brieher1991 y Briere19933. Brieswitz19998>Briggman2003rr Briggs1984 s Briggs1985 +b Briggs19858t Briggs1986<u Briggs1986  Briggs19868 Briggs19868 Briggs1987 Briggs19878 Briggs19898+a Briggs19899 Briggs1992 w Briggs1992 5 Bright1990,F Bright19988/ Bright20000 Brightwell1990  Brigot1992 7 Brik200017 Briknarova20012 Briknarova2001 E Brill19804 Brimacombe200224 Brimacombe20027 Brimacombe20020y Brindle1991 Bringas1992 Brinigar199392 Brinker20003R Brinker20026 Brinker20028| Brinker2002 Brinkmann1992  Brinkmann1993z Brion1991{ Brion1991 Brion1991 Brion1992| Brion1993( Brisson1994 Brito1992! Britton1993* Brive199817 Brive20012 Brive2001Brnjaskraljevic1992~ Broadhurst1991 c Broadhurst19929! 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Brodsky19991 Brodsky1999/ Brodsky20001 Brodsky20001 Brodsky20001K Brodsky20011N Brodsky20011g Brodsky20011 Brodsky20011 Brodsky200137 Brodsky20023 Brodsky20024{ Brodsky20024 Brodsky20039  Brody1994- Broedel1999 Broger1993 + Broglia1998 Broido19911Bromberg1994(Bromberg1995,' Bromme1996 Bron19909# Bron19911 Bron1993v#O Bron199397 Bron2000 Broni1992 Bronson1990k Bronson1991* Broo1998v0HBrookman1995p Brooks1986 "& Brooks19900"' Brooks1991 "( Brooks1991  Brooks1992 Brooks19922") Brooks19922 Brooks1993  Brooks1993  Brooks1993 Brooks19939 Brooks19939#S Brooks19933, Brooks1997) Brooks19981,W Brooks19981- Brooks1998-  Brooks1998/ Brooks199993 Brooks2001<3 Brooks2002U4c Brooks20028 Brooks200225 Brooks20039% Brooks2004V8 Brooks III1987=8 Brooks III1993 Brooks III1995 # Broomesmith1991 A Broomesmith1993.a Broos1999 Brophy19931 Brophy19933 Brophy199336Brorsson1997 Brose19931 Brosh20019 Brost2004HBrostrom1992HBrostrom19922Brostrom1999D2Brostrom1999D Brot19919= Brot1992 Brot19929 Brouillette19925 Brouillette20032.Broutin-L'Hermite1999 Brower1993 4 Brower2003) Brown1971/ Brown1984 Y Brown1985. 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Brown20018s Brown20016 Brown20028r Brown2002 Brownbridge1993,7 Browne1997s Broyde19939 Bruccoleri1990  Bruccoleri1992 Bruccoleri19933) Bruccoleri19955 Brodsky1992' Brodsky1992 Brodsky1992 Brodsky1993 Brodsky1993I Brodsky1993 Brodsky1996* Brodsky1998, Brodsky1998, Brodsky1998, Brodsky1998-8 Brodsky1999 Broger1993 + Broglia1998 Broido19911Bromberg1994(Bromberg1995,' Bromme1996 Bron19909# Bron19911 Bron1993v#O Bron19939 Broni1992 Bronson1990k Bronson1991* Broo1998v Brooks1986 "& Brooks19900"' Brooks1991 "( Brooks1991  Brooks1992 Brooks19922") Brooks19922 Brooks1993  Brooks1993  Brooks1993 Brooks19939 Brooks19939#S Brooks19933, Brooks1997) Brooks19981,W Brooks19981- Brooks1998-  Brooks1998 Brooks III1995 # Broomesmith1991 A Broomesmith1993 Brophy19931 Brophy19933 Brophy19933 Brose1993HBrostrom1992HBrostrom1992 Brot19919= Brot1992 Brot19929 Brouillette1992 Brower1993 ) Brown1971 Y Brown1985. Brown1985 Brown1986 Brown1986 Brown1987 Brown1988 Brown1989 Brown1990 Brown1990' Brown1990" Brown1990 Brown1991 Brown1991 ) Brown1991 Brown1991 Brown1991 Brown1991" Brown1991 Brown1991 Brown1991 R Brown1991 Brown1992 Brown1992 Brown1992 Brown1992 Brown1992 Brown1992 Brown1992 Brown1992r Brown1992 Brown1992 Brown1992%8 Brown19923 Brown1992S Brown1992" Brown1992 S Brown1992| Brown1992 Brown1992 Brown1992 Brown1993 Brown1993 Brown1993 Brown1993 Brown1993 Brown1993 Brown1993% Brown1993 Brown1993 Brown1993 T Brown1993W Brown1993 Brown1993 Brown1995 Brown1996 Brown1996( Brown1996*, Brown1997+ Brown1998, Brown1998 Brownbridge1993,7 Browne1997s Broyde19939 Bruccoleri1990  Bruccoleri1992 Bruccoleri19933) Bruccoleri19955leri19955@AcidyFTGTSTTTTT/T6T7T8T9TTTTTT TT*TQTYTTTTTT/TATVTUTTT T "T $T )T 0T dT T)T T!T!T!%T!$T!]T!T!T!T"/T"BT"LT"oT"T"T"T"T"T"T"T"TofSecASecYEG SolutionStatevan s\ sZP 199837a rbetween BiochemistryCderDoes DriessenE Formationin Inserted Interaction KaufmannLutzMManting Membrane MicellarofSecASecYEG SolutionStatevanP s[0P 201-210istry s[0 s\0  :Ы g,134142199433acidbbinding Biochemistry cellular Equilibriumfolding GieraschJLLiuMofPpredominantlyprotein retinoicRizosheetstudiesZD ? S0z"Zrouting jv<vinenxxw www!w8$w8dw5I'w6ellllandseenyy&ing#sDyEaaaaa(a*aUa(a.a/a/a/ea2Za2[a5|a8'aHalRR=R 0R cR p p ppe e_eee eGeeeTeZe ,c$qc%c+c+c Cc0c7'c7'c chowdhuryer z3&3&3&3&3&3&3&3&3+H3+L3+R3+S3)13) 3+3+_3+f3+g333+i3+l333)23'R33#3+3+3 3+3+3+3+3+3+3+3+3+3+3+3+3+3+3+333%~G%2%2%2%2%2%2%2%2%2%2%2%2& 2& 2& 2&2&2&2&2+2&!2& 2&2&"2&%2&&2&(2&+2&12&42&>2&=2&L2&K2&T2&V2&Y2&e2&u2&t2&|2&2&2)2&2&2&2&2'2'&2+N2)52+\2+^2u2+a2%2+h2+h2+h2+h2+h2+h2&tS&sc&yc&|c&zc)c)c&c&c&c&c'!c'"c'$c+Lc+Qc+Sc+Tc+Uc)3c))c)!c+Xc+Zc+Jc+c+^crcucc+`c+ac+bc%c'Kc+fc+hccc+lc iccQcHcc)Dcc)ccc+oc% c'Rcec+wcw+cw+c+wc+wc+wc+wcw+c+wc+wc P.E. Lerner, R.A. 1988d]Folding of immunogenic peptide fragments of proteins in water solution; II. The nascent helixq 201r1201-217o 5 MayM"Journal of Molecular Biology 1906D>Dyson, H.J. Rance, M. Houghten, R.A. Lerner, R.A. Wright, P.E. 1988Folding of immunogenic peptide fragments of proteins in water solution; I. Sequence requirements for the formation of a reverse turn 201t1161-200 5 May"Journal of Molecular Biology7hstate7js7ns7qs7s7s7s7s7s7s7s7s7s7s7s7s7s8s8s8s8)s82s83s8Js8[s8as8fs8is8zs8}s8s8s8s8s8s8s8s8s8s6s8s+s1O's1Z's1's1's1's1's1's1's2x's2's2's2's2's2's3's3's4&'s4D's4M's4P's4's4's4's4's5G's5H's5T's5o's5's5's5's5's5's5's5's5's6%'s69's6C's6R's6{'s6's6's6's7c's7's7's7's7's7's7's8B's8F's8U's8~'s8's8's8's6's ls o n p r:q+to~(*q*q*q+to~(*qt(cruztystalbll ll)l-l(l'lin zationi  ographica*SysTPuultUREd#niberti@rrentlv3v [vesyanomet"rclasee!ich oo Philinssporinsteine,IqICttOCHromec M r MF M MMEtryplasmicH S* Sj S*K S Skeletono(oliicD"Dea1aa)aSaa ka a a .a a ]a a 3&331993  Russell1993 Russell1993" Russell1996! Russell1996D Russo1989# Russo1991 Russo1991 Russo1992$ Russo1992% Rustici1993d Ruterjans1991- Ruterjans19920 Ruterjans1993 Ruterjans1993$U Ruterjans1993. Ruterjans1996. Rutkat19944g Rutkowski1989 Rutkowski1992&Receptoroooooo5o9oKoeojo$oBosoooo o o .o o o o o o o o!o!Ao!No!fo!o!o!o!o"o"o">o"o"o#Co#Qo#go#o#o$o$o$+o$o$o$o$o$o%,o%Lo%o%o%o%o%o%o%odesign and synthesis of a bifunctional reagent, 1, is described. This compound binds to beta-pleated sheet protein structures, while providing a complexation site for ferrous ion. These immobilized ions may be used to generate reactive, diffusible chemical species at or near the protein surface.ngDesign and Synthesis of a Potential Affinity/Cleaving Reagent for Beta-Pleated Sheet Protein Structuress1h10519-5220*Bioorganic and Medicinal Chemistry Letters 65016/Resnic [SiGnalC M M M M!M! M!M!*M!+M!3M!EM!KM!kM!lM!mM!M!M"M"tM"uM"wM"M#M#+M#3M#?M#OM#M#M#M#M#M$M$*M$NM$zM$M+6M$M$M$M%M%\M%M%M%M%M%M%M%M%M&M&GM&M&M&M&M&M&M&M&M&M1 1=110#q0v0022222 691332T222 2 92$3$3%)33$327 4 4433Y33 34 44y6n6 6 y666 5 5c66!6&c66660364&\3 4 8 + P 1816 Douglas, S.E.p 1992ALGAE BACILLUS-SUBTILIS C-CONTAINING ALGA CHLOROPLAST ENDOPLASMIC RETICULUM CHLOROPLAST TRANSIT PEPTIDES COMPLETE SEQUENCE DNA ESCHERICHIA-COLI EXPORT GENE ORGANIZATION INTEGRAL MEMBRANE-PROTEIN PLASTID RIBOSOMAL-PROTEIN OPERON SECRETION THYLAKOID LUMENeHBA secY Homologue Is Found in the Plastid Genome of Cryptomonas-Phi FEBS Letters 2981 93-96 17 Feb 1817 Douglas, W.W. 1993CURRENTS CYTOSOLIC CA-2 ELECTRICAL-ACTIVITY GLAND ION CHANNELS MELANOCYTE-STIMULATING HORMONE PARS-INTERMEDIA CELLS RAT PITUITARYv82Calcium, Stimulus-Secretion Coupling and Exocytosis -Glancing Back 30 Years - And Recent Lessons on Spontaneous Secretion from Melanotrophs Revealing Calcium-Driven Autonomous Secretion, Independent of Action Potential Discharge, and Its Uncoupling by the Secretacurbins - Dopamine, GABA and Neuropeptide-YBiomedical Researchc14 9-19 1818VPDoukas, A.G. Junnarkar, M.R. Alfano, R.R. Callender, R.H. Kakitani, T. Honig, B. 1984d]Fluorescence quantum yield of visual pigments: evidence for subpicosecond isomerization rates,8115 4790-4794 AugVOProceedings of the National Academy of Sciences of the United States of AmericaB;Douville, K. Price, A. Eichler, J. Economou, A. Wickner, W.n 1995RKSecYEG and SecA are the stoichiometric components of preprotein translocaser&Journal of Biological Chemistrys 27034 20106-20111-4-The transport of large preproteins across the Escherichia coli plasma membrane is catalyzed by preprotein translocase, comprised of the peripherally bound SecA subunit and an integrally bound heterotrimeric domain consisting of the SecY, SecE, and SecG subunits. We have now placed the secY, secE, and secG genes under the control of an arabinose-inducible promoter on a multicopy plasmid. Upon induction, all three of the proteins are strongly overexpressed and recovered in the plasma membrane fraction. These membranes show a strong enhancement of 1) translocation ATPase activity, 2) preprotein translocation, 3) capacity for SecA binding, and 4) formation of the membrane-inserted form of SecA. These data establish that SecY, SecE, and SecG constitute the integral membrane domain of preprotein translocase.c Downard, K.M. 1998Characterization of the conformations of antigenic peptides of protein lactate dehydrogenase (LDH-C4) by electrospray ionization mass spectrometry.0)Rapid Communications in Mass SpectrometryW11 1853-1858  SJE 1828("Doyle, M.L. Weber, P.C. Gill, S.J. 1985PICarbon monoxide binding to Rhodospirillum molischianum ferrocytochrome c'n Biochemistry248 1987-1991S 9 Apr1 1822Doyle, M.L. Gill, S.J. 1985jdStoichiometry determination for carbon monoxide binding to Rhodospirillum molischianum cytochrome c'&Journal of Biological Chemistry 26017 9534-9536 15 Aug 1823.'Doyle, M.L. Gill, S.J. Cusanovich, M.A. 1986HBLigand-controlled dissociation of Chromatium vinosum cytochrome c' Biochemistry259o 2509-2516r 6 May@ 1825:3Doyle, M.L. Gill, S.J. Meyer, T.E. Cusanovich, M.A.b 1987JDThermodynamics of carbon monoxide binding to monomeric cytochrome c' Biochemistry2625 8055-8058 15 Dec 18216/Doyle, M.L. Di Cera, E. Robert, C.H. Gill, S.J.a 1987F?Carbon dioxide and oxygen linkage in human hemoglobin tetramersx 196o4927-934 20 Aug"Journal of Molecular Biology 1820("Doyle, M.L. Di Cera, E. Gill, S.J. 1988Effect of differences in optical properties of intermediate oxygenated species of hemoglobin A0 on Adair constant determinationN Biochemistry272820-824 26 Jan 1824JCDoyle, M.L. Gill, S.J. De Cristofaro, R. Castagnola, M. Di Cera, E. 1989^XTemperature- and pH-dependence of the oxygen-binding reaction of human fetal haemoglobinBiochemical Journal5 2602e617-619 1 Jun- 1827*$Doyle, M.L. Simmons, J.H. Gill, S.J. 1990LFAnalysis of parameter resolution from derivatives of binding isotherms BiopolymersT29 8-9S 1129-1135A 5 Jul-AugNN0  2127,&Fay, S.P. Domalewski, M.D. Sklar, L.A. 1993>8DYNAMICS FLUORESCEIN G-PROTEIN LIGAND REAL-TIME ANALYSISWe have studied the interaction of a family of fluorescent formyl peptides with their receptor using spectrofluorometric and flow cytometric methods. The peptides contained four (CHO-Met-Leu-Phe-Lys-fluorescein), five (CHO-Met-Leu-Phe-Phe-Lys-fluorescein), or six (CHO-Nle-Leu-Phe-Nle-Tyr-Lys-fluorescein) amino acids. As observed in earlier studies, the fluorescent peptides containing four and five amino acids were quenched upon binding to the receptor, while the hexapeptide was not. While the degree of quenching of the bound tetrapeptide was largely unchanged, the quenching of the bound pentapeptide decreased with increasing pH over the range of pH 6.5-9.0. Ligand binding studies have shown that the mole fraction of tetrapeptide or pentapeptide bound in kinetic analysis markedly decreased with increasing pH as a consequence of increasing ligand dissociation rate constant. The dependence of the binding parameters for the hexapeptide on pH was much less pronounced. Over a pH range from pH 7.3 to 9.0, the hexapeptide showed little change in binding affinity, while the tetrapeptide and pentapeptide increased in K(d) approximately 2.0- and 2.5-fold, respectively. These results indicate that the formyl peptide receptor binding pocket contains at least two microenvironments. The pH sensitivity of the pentapeptide quenching is consistent with a protonating environment, while the pH-independent quenching of the tetrapeptide may reflect aromatic stacking or a hydrophobic microenvironment. The pH-dependent ligand dissociation also suggests that the protonation in the pocket stabilizes ligand binding, which may indicate an alteration in the binding pocket structure. Protonation or hydrogen bonding of the pentapeptide may lead to even further stabilization of that ligand.t^WEvidence for Protonation in the Human Neutrophil Formyl Peptide Receptor Binding Pocketd Biochemistry326 1627-1631 16 Feb 2128.(Fayet, O. Louarn, J.-M. Georgopoulos, C. 1986haSuppression of the Escherichia coli dnaA46 mutation by amplification of the groES and groEL genesn 202435-445$Molecular and General Genetics 21292+Fayet, O. Ziegelhoffer, T. Georgopoulos, C.h 1989~wThe groES and groEL Heat Shock Gene Products of Escherichia coli Are Essential for Bacterial Growth at All TemperatureseJournal of Bacteriology 1710 1379-1385  Fgin, C.O. 19954-Unerstanding and increasing protein stability\$Biochimica et Biophysica Actat 1252 1-14 JAH 21316/Feany, M.B. Yee, A.G. Delvy, M.L. Buckley, K.M.S 1993ALPHA-LATROTOXIN RECEPTOR BINDING BIOGENESIS EXOCYTOSIS IDENTIFICATION MEMBRANE-PROTEIN MICROVESICLES PC12 CELLS PLASMA-MEMBRANE SECRETORY VESICLESnThe Synaptic Vesicle Proteins SV2, Synaptotagmin and Synaptophysin Are Sorted to Separate Cellular Compartments in CHO FibroblastsJournal of Cell Biologys 123-3575-584 Nov- 2130 Feany, M.B. Buckley, K.M. 1993~xALPHA-LATROTOXIN RECEPTOR BINDING BIOGENESIS CELLS EXPRESSION IDENTIFICATION NEURONS PC12 CELLS SYNAPSIN-I SYNAPTOPHYSIN`YThe Synaptic Vesicle Protein Synaptotagmin Promotes Formation of Filopodia in Fibroblasts3 Nature 364 6437537-5404 5 Aug 2132D=Feder, J.H. Rossi, J.M. Solomon, J. Solomon, N. Lindquist, S.o 19925' END DROSOPHILA ESCHERICHIA-COLI GENE HEAT-SHOCK HSP70 II TRANSCRIPTION MELANOGASTER MESSENGER-RNA PROTEIN SEQUESTRATION REGULATION RNA-POLYMERASE SACCHAROMYCES-CEREVISIAE SHOCK PROTEIN-SYNTHESISoVOThe Consequences of Expressing hsp70 in Drosophila Cells at Normal Temperaturess68 1402-1413 AugGenes and Developmente*"{"zp"y "w: 7950Trun, N.J. Silhavy, T.J. 1989LEESCHERICHIA GENE INSERTION MEMBRANE PRLC PROTEIN SECA SEQUENCE SIGNALcThe prlC gene product of E. coli can be altered by mutation so that it restores export of proteins with defective signal sequences. The strongest suppressor, prlC8, restores processing of a mutant signal sequence to a rate indistinguishable from the wild-type. Data obtained by changing gene dosage of the dominant suppressor and its specificity for different signal sequence mutations suggest that PrlC8 interacts directly with the hydrophobic core of the signal sequence. Despite the fact that signal sequence processing appears to be mediated by leader peptidase, the processed mature protein is not translocated efficiently from the cytoplasm. Results obtained with various double mutants indicate that PrlC8-mediated processing of mutant signal sequences does not require components of the cellular export machinery such as SecA, SecB, or PrlA (SecY) and that the block in translocation from the cytoplasm occurs because PrlA (SecY) fails to recognize the defective signal sequence. Perhaps PrlC8 directs insertion of the mutant signal sequence into the membrane bilayer to an extent that processing by leader peptidase can occur. This reaction is novel in that it has not been obsd. previously in vivo. 0022-2836ePrlC, a suppressor of signal sequence mutations in Escherichia coli, can direct the insertion of the signal sequence into the membrane 20541665-676oPrinceton, NJ 08544, USA"Journal of Molecular Biology 7953>7Truong, H.T.N. Pratt, E.A. Rule, G.S. Hsue, P.Y. Ho, C. 1991ACTIVE TRANSPORT CONFORMATIONAL STABILITY HYDROPHOBIC CORE MECHANISMS MUTATIONS NUCLEAR MAGNETIC-RESONANCE P22 TAILSPIKE PROTEIN PHAGE-P22 TAILSPIKE PURIFICATION RAMAN-SPECTROSCOPYA combination of site-specific mutagenesis and F-19 nuclear magnetic resonance has been used to investigate the structural properties of D-lactate dehydrogenase, a membrane-associated enzyme of Escherichia coli. The protein (65000 Da) has been labeled with 5-fluorotryptophan for F-19 nuclear magnetic resonance studies. Tryptophan has been substituted for individual phenylalanine, tyrosine, isoleucine, and leucine residues at various positions throughout the enzyme molecule, and the fluorinated native and substituted tryptophan residues have been used as probes of the local environment. All 24 mutants thus generated are expressed in E. coli. Ten are fully active and purifiable following the usual procedure, while 14 either are inactive or produce low levels of activity. The amount of active enzyme produced from the low-yield mutants is dependent on the temperature at which synthesis is carried out, with more active enzyme produced at 18-degrees-C than at 27, 35, or 42-degrees-C. Cells grown at 27-degrees-C and then incubated at 42-degrees-C retain 90-100% of their activity. All of the expressed protein from the inactive mutants is Triton-insoluble, aggregated, and not readily purifiable; the inactive mutant protein appears to be improperly folded. Most of the expressed D-lactate dehydrogenase from the partially active mutants is also Triton-insoluble; a small fraction, however, is soluble in Triton and can be purified to yield active enzyme. All the purified enzymes from these low-yield mutants of D-lactate dehydrogenase have essentially normal V(max)s, and all but two have normal K(m)s. Once purified, the low-yield mutant enzymes are stable at 42-degrees-C. Folding is temperature-sensitive, but once folded, the protein is thermally stable. Thus, in these mutants the tryptophan substitution produces temperature-sensitive folding mutants. The F-19 nuclear magnetic resonance spectra of a majority of these temperature-sensitive folding mutant proteins show abnormalities compared to the spectra of wild type or fully active mutants of D-lactate dehydrogenase, indicating that even though these mutants are functional, their structure is perturbed by the tryptophan substitution.Inactive and Temperature-Sensitive Folding Mutants Generated by Tryptophan Substitutions in the Membrane-Bound D-Lactate Dehydrogenase of Escherichia-Coli Biochemistry3044 10722-10729 5 Nov 7954 Tsai, F.C.S. Sherman, J.C. 1993`ZALPHA-HELIX GLOBULAR-PROTEINS INTERMEDIATE POLYPEPTIDE-CHAIN SECONDARY STRUCTURE STABILITYtnCircular Dichroism Analysis of a Synthetic Peptide Corresponding to the alpha,alpha-Corner Motif of Hemoglobin:3Biochemical and Biophysical Research Communications 1961435-439 15 Oct6/Tsai, C.J. Lin, S.L. Wolfson, H.J. Nussinov, R. 1996nhA dataset of protein-protein interfaces generated with a sequence-order-independent comparison technique 2604604-620d"Journal of Molecular Biology&Tsai, C.-J. Xu, D. Nussinov, R. 1998+Protein folding via binding and vice versa.d     * Folding and Design3R71-R80 SJE Frankel eeJ"iiJi-m$manrirequency*Bund 3ieden#schomu u y-yTy4yyyJyy/y y$=y,y yyyy!6y&y)y%Sy-@y('y ydman uchshjishima:llt#<e$ e" ern #nctionaaoa\a \a8a* a als s d$z sE s) ss* d damentalr#V'rkthers&moree +sion,gG(G+Gs*seGEEhaaa A ]A A A A 2222nRCHEmAe0e0e4e5e6`e6e8e8e8e+Ze+[e+\e,e-e,e0c0c0c0c0c0c0c0c0c0c1c1c0c0c0c8e8e8e6'e7'e8'e9Cbiochemferisii-iicalssss2szssssgssss s s s !s s s*sHsssTsWsWsssssssc0c0c0c0c0c0c1c1c0c0c0c0cferiseii-iicalssss2szssssgssss s s s! s s s*sHsssTsWsWsssssss Early*@s s =s's*s sKsss$s#ss4s9s_s*sHsrsss#s#ds%as%s&ss+s*s(sFs+s,*s&sds+sOs-s*swscs.s.s.ss0's0*s1s)/s1s0ms2ss"s"s2Qs2Ts3s1s4s5{s5s5s6s7ys9>ss `sess s"8s1ss0sRn Yn OnnnMnnn Zn n nr Rather gAgtggtggOg)Gg,g g!'g"Eg"Mg)g%'g%g0g#g5g5g6#g6Zg6}g6g6g7 g7;g7<g7>g7Eg7Kg7mg7g8Tg8cg8yg8|g8g8g*geb*jyinavelu!io!n"n-nn neNN Nn"n+_n-n+n+ nnalii#i.i.i4ii)ii \e+~e8]e$e$ i i+Y i7< i8?ization6} e8  de d'P l8? s8J s8 s6D s6} i6 i6* ing 1ly s s/ ss osnnn Nn-n6&l6l8Ul/oliffn2nnas(swamyswamyswamyswamyPROTEIN PURIFICATION TNF RECEPTORf`Identification of the Binding Site of 55kDa Tumor Necrosis Factor Receptor by Synthetic Peptides:3Biochemical and Biophysical Research Communicationse 1882s503-509 30 Oct 4503Lieberman, M. Sasaki, T. 1991@:CONSTRUCTION DESIGN FOLDING UNITS HELICAL PROTEIN TEMPLATEB;Iron(II) Organizes a Synthetic Peptide into 3-Helix BundlesO.(Journal of the American Chemical Society 1134f 1470-1471n 13 Feb $6$$$p$$B*[$$$> 8445Wice, B.M. Gordon, J.I. 1992A strategy for isolation of cDNAs encoding proteins affecting human intestinal epithelial cell growth and differentiation: characterization of a novel gut-specific N-myristoylated annexinJournal of Cell BiologyB 116`2 405-422 Jan@*$Wiche, G. Oberkanins, C. Himmler, A. 1991JCMolecular Structure and Function of Microtubule-Associated Proteins& International Review of Cytology 124217-273 8446INCOMPLETE BOVINE BRAIN KINESIN CYTOPLASMIC DYNEIN DYNEIN-LIKE PROTEIN FAST AXONAL-TRANSPORT NERVE GROWTH-FACTOR PAIRED HELICAL FILAMENTS PERMEABILIZED MITOTIC CELLS PIGMENT ORGANELLE TRANSLOCATION SEA-URCHIN EGG SQUID GIANT-AXON. 8447*$Wichmann, H. Hengst, L. Gallwitz, D. 1992`ZEndocytosis in Yeast - Evidence for the Involvement of a Small GTP-Binding Protein (Ypt7p) Cell717T 1131-1142A 24 DecWickelgren, I. 1997>7Biologists Catch Their First Detailed Look at NO EnzymeScience  278 389 84542+Wickner, W. Date, T. Zimmermann, R. Ito, K.3 19834-The secretion and assembly of coliphage M13 coat protein into the plasma membrane of Escherichia coli was studied by a method involving growing E. coli cells in a medium with a low concn. of at least 1 amino acid (M9 or M63), infection with M13 virus, pulse labeling with that amino acid ([3H]phenylalanine or [3H]proline), chasing with an excess of nonradioactive amino acid (with or without added drugs for energy poisoning), removal of culture portions at various intervals to an environment that immediately quenches the assembly and processing reactions (e.g., TCA), subcellular fractionation with proteolysis for studying the topog. of distribution across membranes, and identification of labeled bands by SDS-polyacrylamide gel electrophoresis and fluorog. or autoradiog. (after immunopptn., if necessary). 0076-687997(Biomembranes, Part K) 57-61rjcPulse-labeling studies of membrane assembly and protein secretion in intact cells: M13 coat proteinMethods in Enzymology Wickner, W. 1989&Secretion and membrane assemblyd$Trends in Biochemical Sciences147280-283d 8453A review, with 61 refs., on membrane assembly, cytoplasmic protein folding to bury apolar segments, and apolar segments of precursors of secreted and membrane proteins in recognition by membrane receptors and chaperones. 0376-5067 8451 Wickner, S.H. 1990 DNAJ 0027-8424eThree Escherichia coli heat shock proteins are required for P1 plasmid DNA replication: formation of an active complex between E. coli DnaJ protein and the P1 initiator protein877 2690-2694VOProceedings of the National Academy of Sciences of the United States of Americae.(Wickner, W. Driessen, A.J.M. Hartl, F.U. 1991ZSThe enzymology of protein translocation across the Escherichia coli plasma membrane60 101-24 8455A review, with 198 refs., on leader peptides, gene sec protein-dependent and -independent translocation, export energetics, other translocation reactions, and bacterial export. 0066-4154s$Annual Review of Biochemistry 8450*$Wickner, S. Hoskins, J. McKenney, K. 1991 DNAJ 0028-0836TNFunction of DnaJ and DnaK as chaperones in origin-specific DNA binding by RepA 350f 6314165-167 Nature 8449*$Wickner, S. Hoskins, J. McKenney, K. 1991 DNAJ 0027-8424f`Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin8818 7903-7907VOProceedings of the National Academy of Sciences of the United States of America6.-1!" Dec 20HBStructure of the LDL receptor extracellular domain at endosomal pH 2353-8The low-density lipoprotein receptor mediates cholesterol homeostasis through endocytosis of lipoproteins. It discharges its ligand in the endosome at pH < 6. In the crystal structure at pH = 5.3, the ligand-binding domain (modules R2 to R7) folds back as an arc over the epidermal growth 6720 Russell, R.B. Barton, G.J. 1992AMINO ACID SEQUENCES BINDING CHYMOTRYPSIN CRYSTAL-STRUCTURE DEHYDROGENASE DEHYDROGENASE FOLD DYNAMIC PROGRAMMING PREDICTION PROTEIN STRUCTURE COMPARISON RESOLUTION SECONDARY STRUCTURE SEQUENCE ALIGNMENT SIMILARITIES STREPTOMYCES-GRISEUS TRYPSIN STRUCTURE ALIGNMENT{Multiple Protein Sequence Alignment from Tertiary Structure Comparison - Assignment of Global and Residue Confidence Levels142309-323 Oct40*Proteins: Structure, Function and Genetics\URussell, R.G. Graveley, R. Coxon, F. Skjodt, H. Del Pozo, E. Elford, P. Mackenzie, A. 1992JCCyclosporin A. Mode of action and effects on bone and joint tissues60Scandinavian Journal of Rheumatology. Supplement95 9-18 6723 6721 Russell, R.B. Barton, G.J. 1993AMINO-ACID SEQUENCE CRYSTAL-STRUCTURE FAMILY FEATURES GLOBULAR-PROTEINS IDENTIFICATION MEMBRANE-BINDING PREDICTION SECONDARY STRUCTURE SEQUENCE ALIGNMENT SH3 DOMAIN SUBUNIT TERTIARY STRUCTURE`d^The Limits of Protein Secondary Structure Prediction Accuracy from Multiple Sequence Alignment 2344951-957 20 Dec"Journal of Molecular Biology.'Russell, R.B. Copley, R.R. Barton, G.J. 1996JCProtein fold recognition by mapping predicted secondary structures. 259 349-365"Journal of Molecular Biology SJEi2+Russell, C.J. Thorgeirsson, T.E. Shin, Y.K.n 1996`ZTemperature dependence of polypeptide partitioning between water and phospholipid bilayers Biochemistry3529 9526-9532e*#Russell, R. Jordan, R. McMacken, R.RLKinetic characterization of the ATPase cycle of the DnaK molecular chaperone'zDepartment of Biochemistry, School of Hygiene and Public Health, Johns Hopkins University, Baltimore, Maryland 21205, USA.9425082` Biochemistry 1998372596-607.|vhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=9425082 http://dx.doi.org/10.1021/bi972025p60Russell, R. Karzai, A.W. Mehl, A.F. McMacken, R. 1999~xDnaJ dramatically stimulates ATP hydrolysis by DnaK: insight into targeting of Hsp70 proteins to polypeptide substrates. Biochemistry38 4165-4176 SJEd$Russell, S. J. Cochran, A. G. 2000XRDesigning stable beta-hairpins: energetic contributions from cross-strand residues.(Journal of the American Chemical Society 1.9  Jun 12'b[Department of Protein Engineering, Genentech, Inc. 1 DNA Way, South San Francisco, CA 940805Listi6e6e6e6e6e6e6e6e6e6 e6 e6 e6 e6e6e6e6e6e6e6e6e6e6e6e6e6e6 e6!e6"e6#e6$e6%e6&e6'e6(e6)e6*e6+e6-e6.e6/e61e62e63e64e65e66e67e68e69e6:e6<e6=e6?e6@e6Ae6Be6Ce6De6Ee6Ee6Ee2m Structure2s s2u s2w s2 s2 s2 s2 s2 s2 s2 s2 s2 s2 s2 s2 s3 s3 s3 s3! s3& s3 s32 s3c s3` s3\ s3[ s3Z s3l s3m s3o s3 s. s3 s3 s3 s3 s3 s3 s3 s3 s4  s4 s4 s4" s4$ s4% s4- s4+ s4; s4A s4J s4e s4n s4j s4 s4~ s4) s4t s4t s4t s4t s4t s, M. Hinz, H.J. Scharf, M. Engels, J.W.o 1992ACCESSIBLE SURFACE AREA AMINO-ACID RESIDUES AQUEOUS-SOLUTION GEOMETRY GLOBULAR-PROTEINS HEAT-CAPACITY HYDROPHOBIC INTERACTION NUCLEAR MAGNETIC-RESONANCE PANCREATIC TRYPSIN-INHIBITOR STABILITY TENDAMISTAT THERMODYNAMICS UNFOLDING VOLUMESThermodynamics of Unfolding of the alpha-Amylase Inhibitor Tendamistat - Correlations Between Accessible Surface Area and Heat Capacity 2233769-779 5 Feb"Journal of Molecular Biology*133027717!74 4(7 9f2!$3,3.33(3f734-X4944f4@489^88o85%444o4p5#p60p04P7377A908.98992-+2.454O69)9.50-+0"81O5*6"870A4&@4717!74 4(7 9f2!$3,3.33(3f734-X4944f4@488o85%444o4p5#p60p04P7377A908.98992-+2.454O69)9.50-+0"81O5*6"870A4&@4Indicateed d d d dd_d5dJdtdZdddd^ddhd'ddd$ddlddod~ddd _d!d!d"xd"wd#d$&d$d%d&_d)(d),d+Zd+\d+ed+qd+sd0d0d0d0d0d1d5d6d6d6d6-d68d6Nd6`d6pd6sd6td6d6d6d6d6d6d6d6d7d7 d7%d7)d7-d71d72d73d7Xd7]d7^d7sd7}d7d7d7d7d7d7d7d7d8d89d8Cd8Ud8qd8wd8d8d8d8d8d8d8dmd u# u7 u u u id0d0d1d5d6d6d6dmd u# u7 u u u i8Sci8e6e8*e8,e8-e8/e84e86e8Ae8be8ie8e8e8e8e8e8e8e8e8e8e8e8e8e8e9#e9'e91e9*e93e94e9&e9Pe9Qe9Re9,e9Se7e9be"xe6ejeea a aa$a"Ma69a6a6a7a7/a-za+a5w'a6'a ancaleporedzdmore'encess-s/s3s5s s!sQs*jshsyssss*csssss*sss*bs*s&s/s0s(sTszdmore'encess-s/s3s5s s!sQs*jshsyssss*csssss*sss*bs*s&s/s0s(sTs\%H%a&1a&>a&Oa+a+aa,aanapaa a-taa-a.>a.a/aa/ba+a#'a#$a#%a0a1a/a2Ma2Oa2a3a3;a3Ua4a4a(a*a5a5a6;a6[a6^a7/a71a72a7Qa7a8,a8aa8za8a8a8a-a a2 a a a aA ab a a- a/ aa$aGaJaIaHaKaVasasaa at-aa-a>.a.a/aab/a+a'#a$#a%#a0a1a/aM2aO2a2a3a;3aU3a4a4a(a*a5a5a;6a-a a2 a a a a aA ab a a- a/ aa$aGaJaIaHaKaVasa3236 6 d6 6M66e66B6646 A6!6#j6'T6!96 63646466R6666g6!)6"64g64f64e64t6567o6866N6 6j6 0+65'16{'18'1"Z1 2 2 351119514 4 5T6k4 7 7$Q8 9 945 555555 A5$5' 5557077 <7700%0%0c+Sc+Tc*jcxcc%c%c%c%c%c%c%c%c%c%c%c%c%c)c%c%c&c&c&c&c&c&c&c&7c&Dc&Cc&Bc&>c&Kc+3c&[c&\c&`c&ac&ec&c*jcxccNITIwRNAxz3zScccK[L)C` )YW|+ }~)))G "-Ry %p*%&I"_I"I"I"I"I"I"I#I#I#I#I#&I#.I#EI#fI#I#I#I$I$I$%I$)I$*I$>I$ZI$bI$fI$I$I$I$I$I$I) I$I$I$I%I%(I%,I&I)I%tI*I%I%I%I%I%I%I%I%I%I&I)1I&2I&7I&>I&LI&KI&OI&bI&toC bb,b4b7bCbdbgb)b)b&bbbbbb b Nb Yb Zb [b \b _b b b b b b b!b!'b!Db!fb!ob!nb!b)b!b!b!b!b!b"b"4b"Cb"Eb"Mb"ub"vb"xb"wb"yb"b"b)b# b#b#b#/b#0b0#b#0b#0bT"T"T"T#(T# T#T#;T#IT#ST#TT#^T#~T#T$3T$T% T'ZT%yT%T&)T&+T&[T&T&T+MT#TTTt[TT)TTTTTTTTTTTTTTTTTTT T TT uT T!T!$T!ET!T!T#TTTtWhichllll;l=lxllll l ll}ll)$lRleljlvllllll$l'lXllllll#l*llllolll ll4lCldl)l)llllll Nl \l _l l l l l l l pathway of which the sec gene products are essential components. Removal or drastic alteration of the prepullulanase signal peptide cause the enzyme to remain cytoplasmic. Evidently, pullulanase secretion occurs in 2 steps, the first of which is common to all signal peptide-bearing precursors of exported and secreted proteins, whereas the second is specifically involved in translocating pullulanase to the cell surface. g_P 0 gX 3^BB: 4389@9Leontiev, V.V. Uversky, V.N. Gryaznova, O.I. Gudkov, A.T.P 1993Effect of Single Amino Acid Replacements on T4 Phage Lysozyme Stability .2. Point Mutations ASP10->HIS, ASN101->ASP, ARG148->SER Lead to the Molten Globule Statei Biofizika 3844606-610`Jul-Aug 4391,&Leopold, P.E. Montal, M. Onuchic, J.N. 1992$CHAIN CONFORMATIONS STABILITYZTProtein Folding Funnels - A Kinetic Approach to the Sequence- Structure Relationship8918 8721-8725 15 SepVOProceedings of the National Academy of Sciences of the United States of America 4392.'Lepock, J.R. Frey, H.E. Hallewell, R.A. 1990JCDIFFERENTIAL SCANNING CALORIMETRY INACTIVATION THERMAL-DENATURATIONfContribution of Conformational Stability and Reversibility of Unfolding to the Increased Thermostability of Human and Bovine Superoxide Dismutase Mutated at Free Cysteinesc&Journal of Biological Chemistry1 26535 21612-21618  15 Dec 4393,%Lepock, J.R. Frey, H.E. Ritchie, K.P. 1993ABNORMAL PROTEINS CHL-V79 CELLS DEGRADATION DIFFERENTIAL SCANNING CALORIMETRY HYPERTHERMIA INHIBITION INVOLVEMENT STRUCTURAL TRANSITIONS THERMAL-ANALYSIS THERMOTOLERANCEed]Protein Denaturation in Intact Hepatocytes and Isolated Cellular Organelles During Heat ShockJournal of Cell Biologyr 122061 1267-1276 Sep  4394,&Lepore, L.S. Ellena, J.F. Cafiso, D.S. 1992BILAYER-MEMBRANES BIOLOGICAL-MEMBRANES C-13 CHOLESTEROL DIPOLAR RELAXATION MODEL MEMBRANES NMR NUCLEAR MAGNETIC-RESONANCE ORDER SPIN-LATTICE RELAXATIONS^XComparison of the Lipid Acyl Chain Dynamics Between Small and Large Unilamellar VesiclesBiophysical Journali613g767-775a Mar 4395Lerner, L. Horita, D.A. 1993ngASSIGNMENTS BINDING DISTANCE GEOMETRY ESCHERICHIA-COLI NMR-SPECTROSCOPY PROTEIN-STRUCTURE DETERMINATIONN\VTeaching High-Resolution Nuclear Magnetic Resonance to Graduate Students in BiophysicsBiophysical Journaln656l 2692-2697 Dec` 4396D=Leroux, A. Berebbi, M. Moukaddem, M. Perricaudet, M. Joab, I.e 1993vpACTIVATION BAMHI-E REGION CD23 CELLS DOMAINS EBNA3B EXPRESSION GROWTH-TRANSFORMED LYMPHOCYTES LOCATION PROTEIN-2xqThe Epstein-Barr virus nuclear antigen 3A is expressed in the nuclei of cells latently infected by the Epstein-Barr virus. We have previously shown that a fragment of 265 amino acids was essential for the proper subcellular localization of the Epstein-Barr virus nuclear antigen 3A. As described in this paper, we have used deletion analysis to identify a decapeptide, RDRRRNPASR, which is essential for nuclear localization of this protein. Furthermore, this decapeptide is a functional nuclear localization signal as demonstrated by its ability to target expression of beta-galactosidase in the nuclei of transfected cells.Identification of a Short Amino Acid Sequence Essential for Efficient Nuclear Targeting of the Epstein-Barr Virus Nuclear Antigen-3AJournal of Virologyi673 1716-1720 Mar- 43972,Leroy, J.L. Gao, X.L. Gueron, M. Patel, D.J. 1991ZTProton exchange and internal motions in two chromomycin dimer-DNA oligomer complexes Biochemistry3023 5653-5661 11 Jun SJEIRKLesieur, C. Cliff, M. J. Carter, R. James, R. F. Clarke, A. R. Hirst, T. R.J 2002d^A Kinetic Model of Intermediate Formation during Assembly of Cholera Toxin B-subunit Pentamers J Biol Chem 277+19 16697-704.11877421 JAHuhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11877421 http://www.jbc.org/cgi/content/full/277/19/16697 http://www.jbc.org/cgi/content/abstract/277/19/166977 4401Lesk, A.M. Chothia, C. 1980How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. 1363c225-270e 25 Jan"Journal of Molecular BiologyMODELsI+ rr1rer @r r r r /r)r fr r cr r r)rrrdrrrerrr*rr0r8r)GrGr)rmrUr^rrrrrr r"r"r"r)r)r#qr#r#r$r%sr%tr&r)r)&r)'r)5r)*r+Zr+r+_r+ar+aro%o%o%o%o%o%o%o%o%o&o&+o&3o&Ao&@o&~o)%o)&o)'o)5o))o+Zoo+^oro+_o+ao+bo+coo&o)Doo+xo#o+o+o"oo,o,ooo/o/o)o#oo"oCoo o#Fo#Vo#ao#o#o#oo#o#o#o$}o$o$^3HTbin3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L3L4L4L4L4L4L4L4L12L1L3iL1L1L2L2L20L1L2WL2L1L1e6Ne6ZLLVpp pLp&o13m1@l2l2~l2l/l/o1Uo1\o1_o1`o1ko2o2o2o2o2o20oom20p =pG8R"R8RR RYY&Y&YkY2rAbbkbhbbSS6SMS1t7 tp5u8u+ u+ u+Xu+Zu+[u+\u+\u+\u+\uY2rAbbkbhbbSS6SMS1t +tp +uX+uZ+u[+u\+uu.>L.D1.L1.N1.O1.R1.S1.[1.^1._1./1.81.`1.f1.k1.g1,1.51.1"(1.1.1.1-1.1.1.1-11N1#x1(1.1.1.1.1.1.1.1.1/1/1&1w11/111s1/1/1/1-1 1'S181-]1//1//1//1//1//1//1//1rtfeld1992 Barth1990~ Barth19914 Barth1992 Bartholdi1976B Bartholmes1991  Bartholomeus1992 Bartik1993 Bartlett19911Bartlett19919-C Bartner1998!k Bartoldus1990 Barton19922 Barton19922 Barton1992  Barton19933 Barton19933 Barton1993  Barton1994 " Barton19966+J Barz1998 ' Barzu1990 Barzu1992 Barzu1993: Barzu1993$O Barzu)PO1b1l1t11111^1x111 1=1)1)1&11111111 B1 E1 1 1 1 1 1 1!1!1!!1!41!31!Q1!P1)1!1!1"f1)1)1#R1#b1#q1#1)1$1%1%,1%01%r1%s1%t1%1%1%1%1%1&1s Models, Biological Neurodegenerative Diseases/metabolism Peptides/chemistry Protein Conformation *Protein Foldinge`Zhttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.biomednet.com/article/sba11094195741&Mizuguchi, K. Kidera, A. Go, N.NGCollective motions in proteins investigated by X-ray diffuse scattering Computer Simulation *Crystallography, X-Ray Fourier Analysis Human Models, Theoretical *Motion Muramidase/*chemistry Protein Conformation *Scattering, Radiati Cell$ s s s s s s! s! s!ss!s"s"Zs"es"ss"ts"s"s)Hs"s"s"s"s#s#"s#4s#?s#As#Ys#os#s#s#s#s#s$ s$s*Js$s$ s$1s*s$gs$ks$ns$os$s$s$s$s+6s$s$s$s)s$s$s%s%&s%+s%8s%Ls%MsGHeatmrsts~ssssss'sXszsssss ssssssssss Ps is s!s!,s!?s!Ns!as!s!s!s!s""s"#s"bs"s"s"s"s#9s#Ys#^s#{s#s#s#s$s#s$s$?s$ps$s$s$s$s$s%s%N%6a*a%Aa%Ca%Ba%Ea%Ua%a%a%a%a%a%a%a)a%a&a& a&a&a&&a&Ca&Ba&Ma&Oa*a&Ya&da&ea&a&a&a&ha&ga&fa&a&a&a&sa&ya&a'a'$a+Oa+Qa+Sa),a iaa% a+xa+a+a+a+a+a+a+a+a+a+a+a+a"@"@@4"A4"A"A"AL"A:"A l"A6H"A+8"@"@m"Ay" A"A!"AP"$A(",@a "4@"<@@"D@"L@@"T@4"\AĐ"d 6 7  Biochemistry24 7257-7262 4027Kohanski, R.A. 1993ACTIVATION BASIC POLYCATIONS BETA-SUBUNIT DOMAIN ENDOCYTOSIS EXPRESSION PHOSPHORYLATION PROTEIN-KINASE PURIFICATION TYROSINE KINASEaInsulin Receptor Autophosphorylation .2. Determination of Autophosphorylation Sites by Chemical Sequence Analysis and Identification of the Juxtamembrane Sitesi Biochemistry3222 5773-57805 8 JunVN Dobson1994 M Dobson1994  Dobson19949; Dobson19949 Dobson19941 Dobson19949 Dobson19944e Dobson1994u Dobson199446 Dobson19949'H Dobson19959'C Dobson19959*p Dobson1995 'D Dobson1995  Dobson19959 Dobson19955] Dobson19959'@ Dobson19951% Dobson19951 Dobson19959 Z Dobson19959+ Dobson199550 Dobson19955 Dobson19966 Dobson19969* Dobson19966_ Dobson19969 Dobson19969 Dobson19969& Dobson199614 Dobson19969( Dobson1997( Dobson1997 +" Dobson19977* Dobson19977) Dobson19979( Dobson19979( Dobson19979'' Dobson19977( Dobson19977( Dobson19977( Dobson19977& Dobson19977'_ Dobson19977-A Dobson1997+ Dobson19989) Dobson19989) Dobson19989) Dobson19989+W Dobson1998 + Dobson19988+ Dobson19988+ Dobson19989+ Dobson19989+ Dobson19988, Dobson1998r,+ Dobson19988, Dobson19989- Dobson1998 - Dobson199897[ Dobson19988, Dobson1999-r Dobson19999-v Dobson1999- Dobson19999- Dobson19999- Dobson19999- Dobson1999 - Dobson19999- Dobson19999.1 Dobson19999.5 Dobson1999c.9 Dobson19999. Dobson19999. Dobson19999/p Dobson199990 Dobson199996 Dobson199997 Dobson1999g/] Dobson20000/_ Dobson20000/ Dobson20000/ Dobson20000/ Dobson20000/ Dobson200000 Dobson200000 Dobson200006 Dobson200007A Dobson2000g0 Dobson20012^ Dobson20012` Dobson2001<3 Dobson200116 Dobson20017 Dobson20012 Dobson200203, Dobson200203I Dobson200204X Dobson200224l Dobson20027 Dobson200207 Dobson20027 Dobson20027 Dobson200224 Dobson200335q Dobson200306 Dobson200307 Dobson20037 Dobson2003382 Dobson200308? Dobson200338 Dobson20038 Dobson200338 Dobson20039D Dobson20040" Dodd19911( Dodd19971O Dodge1996c Dodson19822c Dodson19822P Dodson1989 % Dodson19898 Dodson1992s Dodt19891 Doebele19947 Doere2003Q Doering1991R Doering1996# Doherty1991 Doherty1991*W Doherty1997S Dohlman1991%Dohlsten19966 Doi1990T Doi1992 Doi1993U Doi1993 Doi1993% Doi1993, Doi1998W Doig1990vV Doig1990vY Doig1991vZ Doig1992v Doig1993t- Doig1995,V Doig19979. Doig199993D Dokholyan20025t Dokholyan2002\ Dokoh1981+ Dokurno19986 Dokurno2000 Dolan1990 Dolan1990 Dolan1991^ Dolan1991% Dolan1991 Dolan1991_ Dolan1992" Dolgikh1978a Dolgikh1981` Dolgikh1981U Dolgikh1983b Dolgikh1984d Dolgikh1985e Dolgikh1991 Dolgikh1992f Dolgikh1993- Dolgikh1996. Dolgikh199927 Dolgikh2001g Dolginova1992) Dolis1996w Dolja1991 Dolja19922 Dolja2001- Dolla1999h Dolman1978 *Domaille1991Domaille19921Domaille19921!Domaille19921*Domaille1992'UDomaille19969 Domalewski1993 iDomanico1993 Dombrosky1991 Dombrosky1991  Dombrowsky1991  Domchek1993| Domenighini1993" Domer1993 Domingo1993/ Domingo2000 Dominguez1991h Dominguez19936# Dominguez2003jDominici19939g Dominy200103 Dominy2002U% Domoto19909k Doms1993v  Donaldson1984* Donaldson1990#z Donaldson1991 Donaldson1992? 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Dobson19999p/ Dobson199990 Dobson19999]/ Dobson20000_/ Dobson20000/ Dobson20000/ Dobson20000/ Dobson20000/ Dobson200000 Dobson200000 Dobson200000 Dobson2001^2 Dobson2001`2 Dobson2001<3 Dobson20011,2 Dobson200222 Dobson20020,3 Dobson20020I3 Dobson20020X4 Dobson20022" Dodd19911( Dodd19971O Dodge1996c Dodson19822c Dodson19822P Dodson1989 % Dodson19898 Dodson1992s Dodt19891 Doebele1994Q Doering1991R Doering1996# Doherty1991 Doherty1991W* Doherty1997S Dohlman1991%Dohlsten19966 Doi1990T Doi1992 Doi1993U Doi1993 Doi1993% Doi1993, Doi1998W Doig1990vV Doig1990vY Doig1991vZ Doig1992v Doig1993t- Doig1995V, Doig19979. Doig19999D3 Dokholyan2002\ Dokoh1981+ Dokurno1998 Dolan1990 Dolan1990 Dolan1991^ Dolan1991% Dolan1991 Dolan1991_ Dolan1992" Dolgikh1978a Dolgikh1981` Dolgikh1981U Dolgikh1983b Dolgikh1984d Dolgikh1985e Dolgikh1991 Dolgikh1992f Dolgikh1993- Dolgikh1996. Dolgikh199972 Dolgikh2001g Dolginova1992) Dolis1996w Dolja1991 Dolja19922 Dolja2001- Dolla1999h Dolman1978 *Domaille1991Domaille19921Domaille19921!Domaille19921*Domaille1992U'Domaille19969 Domalewski1993 iDomanico1993 Dombrosky1991 Dombrosky1991  Dombrowsky1991  Domchek1993| Domenighini1993" Domer1993  Domingo1993/ Domingo2000 Dominguez1991h Dominguez1993jDominici19933 Dominy2002U% Domoto19909k Doms1993v  Donaldson1984* Donaldson1990z# Donaldson1991 Donaldson1992? Donaldson1993  Donaldson19931 Donaldson20012 Donaldson2002l Donehower1992m Donehower1993y Donehower1993  Donehower1993  Donehower1993( Donelladeana1993&Donelson1993 Dong19909p Dong1991ve Dong19919Y Dong19919n Dong1992n Dong19929o Dong1993v Dong19931 Dong19933|& Dong19933-, Dong199792 Dong1999i1 Dong2001p3 Dong2002' Doniach1993p Doniach1995( Doniach1995&Kihlgren19933/ Kiick2000 Kiino1984 Kiino1990 Kijima1993 ! Kikuchi1988 Kikuchi1990! Kikuchi1990! Kikuchi1990!z Kikuchi1990 Kikuchi1990 Kikuchi1991 N Kikuchi1991! 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King19909 King1991v King19919King19919& Jimenez,Pbb5b7 b'1barbero)nez)n&n)n4n)n8!inan`d1;dIdalbgg/L sskoot6L'kelly7x'im9VL.f)%M)&M)'M)6M)5M)4M)(M)+M),M)-M)3M)1M))M) M)!M)#M)*M+XM+ZM+[M+\M+JM+]M+M+MM+^MMrMuMMM+_M+`M+`MT4źPp1996backcommentNaturenewsPPowersProtein ribosomeTtalks targetingWalter`żp1ENGLANDlterżP1Naturen targż0 @talks back [; comment]1996 @ENGLAND%zBiological Transport Endoplasmic Reticulum Guanosine Triphosphate GTP Phosphohydrolase Protein Binding Proteins Ribosomes Signal Peptides Sign 300*l000 C000001.010 02G02w050608P0 00)0o0+f0+ 06H06W06b06h0708080805`'06'0 0 1 23%3"3663737373,3 44 5$25 6,169,9,6 7 7 8 17'97'99 1222128#12k2 2 B2 *2'2222*222#2#2$+2$2&-2&|22*2/<2-212242224F27u22*2 2 y2;0+0+0002?030)07080P07g0 18'1%1 2$22 3 3 4 4 4+aM+bM%M@M=M'LM2M'KM+cM+dMMMWas e,e4e7edege)e&eeeee Ye [e e e e e e!e!'e!fe!oe!ne!e!e"e"2e"4e"ue"ve"e"e"e#e#e#0e#^e#qe#e#e#e$&c$c$c%c%c&/c&0c&Oc&_c&c)+c)*c+[c+\c+_c%c+dc+dc+dc+dc+dc?1V444D4444Z44>40x #1  4!94"G4"4#(4#4#4#4#4#4$4$U4&Z4"x4`4xZ?1V444D4444Z44>40x #1`ResultstthttttMtOtttttxtt tztytt)$t%tMttt$tzzz)zzzoz~zzzzz4zdzz Nz _z z z z)z!z"z"Mz"vz"xz"wz#0z#zz#z#z$&Y$QY%r&/r/&r&/r&/rColon, W. Roder, H. 1996JKinetic intermediates in the formation of the cytochrome c molten globule 9 ;  Nature Structural Biology3 12 1019-1025 SJE2+Colon, W. Wakem, L.P. Sherman, F. Roder, H. 1997VIdentification of the Predominant Non-Native Histidine Ligand in Unfolded Cytochrome c U V  Biochemistry3641 $BG$K2$Q2$R2$_2$`2$a2$b2$2$2$2$2$2$2$2$2$2$2$2$2$2$2$2$2(2$2$2$2$2$2$2$2$2%2%2%2%2% 2%2%2%2%2%"2%#2%%2&2%52%E2%G2%H2%I2%L2%M2%Z2%_2%^2%b2%a2a%2%a2%a2%a2%a2%a2$1$1'Z1%1%M1%r1%s1%t1%1%1'P1%1%1%1&1&1&01&>1&1)1'!1)%1)&1)41)(1)+1),1)-1)11))1).1)*1+X1"1C11)1 11" 1"1"1"1"1"1)/1)1#1#1#31#41)1#L1#R1#q1#1"1C11)1)'1 11$H$a$a)a$a%a%a%a%a%a%a%a%(a%2a%Aa%Ca%Ba%La%Ta%Wa%Va%Xa%Ya%Za%`a%^a%]a%aa%sa%va%}a*a%a%a%a%a%a%a%a%a'Wa%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%aWI E_  saphicUUSTmetric) a H al W E,GRB2H dadolnike e-eadytat_e)&eEerg&gggl xlEl*llhhh~hh h#qh+[stuThouse) l Elye eheue/e e e eMcbbb)b;bbc co ekgnnngMEMBRANEH s5s6sJsestsXsssss ssss$s#sxsys~ssssstssps s$shssssssssMsOsasssssoooo oo)$oQoeojoooooooooional NMR and distance-geometry/restrained molecular dynamics calculations. The wild-type and aromatic-swap analogue each contain an N-terminal beta-sheet and a C-terminal alpha-helix (beta-beta-alpha motif), as observed in other systems, and exhibit a highly ordered hydrophobic core in which the native or swapped aromatic ring is closely packed. Remarkably, however, the two structures are stabilized by alternative aromatic-aromatic interactions, which in turn alter the respective DNA-binding surfaces. Journal of Biological Chemistryf 26720 13910-13916 15 Jul 4005LFKo, K. Bornemisza, O. Kourtz, L. Ko, Z.W. Plaxton, W.C. Cashmore, A.R. 1992zsBINDING ESCHERICHIA-COLI DNAK GENES HSP70 IMPORT MEMBRANES MESSENGER-RNA POLYPEPTIDES TRANSIT PEPTIDE TRANSLOCATION~wIsolation and Characterization of a cDNA Clone Encoding a Cognate 70-kDa Heat Shock Protein of the Chloroplast EnvelopeN&Journal of Biological Chemistrye 2675 2986-2993 15 Febv SUBstituentsN6 tvte" d1< d d+o d6  d6p d7 d d1 i2 i i $ i % i  i  i \ i ^ ir if i ip i  i' i  i i- i, i i i V i  i  i i' i iv i! i"y i# i6: i6D i6 i6 i7 i7I i  ing o onsQ s u  i vw o t  ]  S S  Y \ e  ib i if i| X h 1 2a $ %    \! ^"B f" # .#q -% % &' &\ & I V V* V| V,g V. -  /Q /v 0 3) 3   5f 75 7   * S. -  n i   Y \ e  ib i| i if i iLysozymezsys{ss6s7As7s8s8 s82s8ds8s8ssL yM y  y y y y7 y y y+ y! y" y$5 y, y y y6 y ylt tttEt6&t tic $M7MM|M~M}M"M+M-M.RM0 M1M3M!MbMMM2u%u&aUU!USruWMYMXM[MZM\M&rM9bartsev6hovitskyMaaaa A A A a(aaaaaa#a,a3a8a)a:a;a=auWMYMXM[MZM\MMaaaa A A A a(aaaaaaa"a#a,a3a8a)a:a;a=aMPROducedgnrrrrjrXrlrr!r"yr$Qr'PrOr0r6Br6Lr6`r6fr6r7r7r77r7r7r7r7r8r8rrsss+[iti ii"yi6i7si8iing t t t"E t& t6 t7 tAt+/iiiqi Ri i Xi i i i i i i i iiiiiiiiiiii i!i!Wi"i%i&ei+i3i4{i6Li6i8iivi t"E tAt+/iiiqi Ri i Xi i i i i i i i iiiiiiiiiiii i!i!Wi"i%i&ei+iivi0}Ofc0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0|N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0NN0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N0N9+9,9,9,9,9,9,9*9,9-9+9+9-9- 9-9-9-%9,9+9-*9,9,99,9,9+;9+9*9- 9,9*9,!9-99,9-@9,9-C9-I9-J9-L9,9,9*9-S9*9-f9-i9-n9-{9-9-9-9-9-9'39*9+Y9,9,9,9T9,9,F,F,  respectively  i  i i iw i iZ i i i i i$ i' i i)$ iQ i i) i  i$U i% i)- i+g i i+ i+Y i0 i)/ i6 i6 i6% i6) i6N i6W i6^ i6f s6 s6 s6 s6 s6 s7 s7 s7c s7h s7s s7t s7 s7 s7 s7 s7 s8a s8| s8~ s8 s8 s8 s8 s8 s6`siration O~ O"ORY~ o o o o6 o~ond2&ss8@s7sseiiiii Bi i i i ii)ibiqiiii9ieifigii $믵($껵  ! ! *D!n Refoldings gK g g g g g g/ g g g g g g g g gH g. g/ g g g g< g9 gj g g_ g gY g g g g g& gn gs g2 g g g gU g g g g  g l g p g  g  g!  g!@ g" g" g) g#y g$ g% g& g& g& g& g( g  " ! 省퀂!"뻿!  % *ﾯ  $ $  $"! !""  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Marszalek1999 Martel1990 Martens1993 Martensson1993 , Martensson1995 Marti1992o Marti1992 Marti1993 Martial1993 8 Martial19934j Martial2003+{ Martienssen1997 Martin19899 Martin19900 Martin1990  Martin1990 8 Martin19909 Martin19919 Martin1991  Martin1991  Martin1991  Martin19919 Martin1992  Martin1992  Martin1992 Martin1992w Martin1992 $ Martin1992 Martin19929 Martin1992 Martin1992  Martin1992  Martin19922 Z Martin19922h Martin19922$ Martin1992 Martin19939 Martin1993 3  Martin1993  Markley1993 Markley1993 Markley1993 Markley1996#q Markley1996* Markley1998 Marks1987 Marks1991 Marks1992* Marks1998) Markus1997 + Markus1998 W Marky1990% Marky1993 Marlow1993  Marlton1993 Marmorino1993 Maron1971! Marotta1992 $ Marquardt1992 Marquardt1993 Marque1984  Marquezmagana1992DMarqusee19855Marqusee1987Marqusee1989bMarqusee19909AMarqusee1991Marqusee19969>Marqusee1996(Marqusee19979(Marqusee?1997 Marra1991 Marraud1991 Marraud1992 Marraud1992E Marraud1992 Marraud1992" Marraud1992 Marraud1993" Marraud1993 Marraud1993 Marsch19922 Marschner1992 Marsh1990? Marsh1991 Marsh1992 Marsh1992 Marsh1992 Marsh1992$1 Marsh1992 Marsh1992 Marsh1992 Marsh1993 Marsh1993  Marsh1993g Marsh1996*H Marsh1997 Marshak1993 Marshall1990 Marshall19919Marshall1991Marshall1991Marshall1992 Marshall1992&Marshall1992mMarshall1992Marshall1992Marshall1992Marshall1992Marshall19933Marshall1993Marshall19931Marshall19931Marsters19922c Marszalek1991 Martel1990 Martens1993 Martensson1993  Marti1992o Marti1992 Marti1993 Martial1993 8 Martial1993 Martin19899 Martin19900 Martin1990  Martin1990 8 Martin19909 Martin19919 Martin1991  Martin1991  Martin1991  Martin19919 Martin1992  Martin1992  Martin1992 Martin1992w Martin1992 $ Martin1992 Martin19929 Martin1992 Martin1992  Martin1992  Martin19922 Z Martin19922 Martin19939 Martin1993 993 1993 Tx/]|.4)T) ^ 7230)Boscott, P.E. Barton, G.J. Richards, W.G. 19931.7-A RESOLUTION 3-DIMENSIONAL STRUCTURE ALIGNMENT CHYMOTRYPSIN COMPLEX DEHYDROGENASE GLOBULAR-PROTEINS HOMOLOGY PREDICTION PROTEASE REFINED CRYSTAL-STRUCTURE SECONDARY STRUCTURE SEQUENCE ALIGNMENT SEQUENCE DETERMINATION>8Secondary Structure Prediction for Modelling by HomologyProtein Engineeringi6P3261-266a Apr0 7240*Bosenberg, M.W. Pandiella, A. Massague, J. 1992tnThe Cytoplasmic Carboxy-Terminal Amino Acid Specifies Cleavage of Membrane TGFalpha into Soluble Growth Factor Cell717 1157-1165 24 Dec 725|Bosman, G.J.C.G.M. Stekhoven, J.H.S. Melenhorst, J.J. Vanzuylen, A.J. Bartholomeus, I.G.P. Vankalmthout, P.J.C. Degrip, W.J. 1992ALZHEIMERS-DISEASE BLOOD CHOLESTEROL DEMENTIA ELECTRON-MICROSCOPY FATTY-ACIDS FIBROBLASTS FREE CALCIUM FREE-FLOW ELECTROPHORESIS HETEROGENEITY HUMAN-PLATELET SURFACE INTRACELLULAR MEMBRANES KINASE MEMBRANE MULTI-INFARCT DEMENTIA PHOSPHORYLATION PROTEIN KINASE-C THROMBOCYTESf_Are Thrombocyte Membranes Altered in Alzheimer's Disease - A Morphometric and Biochemical StudyHNeurobiology of Aging-136g711-716Nov-DecBost, S. Belin, D. 1995{A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery EMBO Journal1418 4412-4421Bost, S. Belin, D. 19976/prl Mutations in the Escherichia coli secG Gene&Journal of Biological Chemistrya 272r7 4087-4093 726"Boswell, D.R. Carrell, R.W.g 1988*#Genetic engineering and the serpins, Bioessayse82  83-87.Feb-MarLEBothner-By, A.A. Stephens, R.L. Lee, J.-M. Warren, C.D. Jeanloz, R.W.i 1984haThe CAMELSPIN-experiment (Cross-Relaxation Appropriate of Minimolecules Emulated by Locked Spins).(Journal of the American Chemical Society 106d811-813 KSR 727Botstein, D. Shortle, D. 1985:3Strategies and applications of in vitro mutagenesispScienceP 229 4719 1193-1201. 20 Sep 728:4Bottaro, D.P. Fortney, E. Rubin, J.S. Aaronson, S.A. 1993CLONING EXPRESSIONrkA Keratinocyte Growth Factor Receptor-Derived Peptide Antagonist Identifies Part of the Ligand Binding Site&Journal of Biological Chemistry3 268o13 9180-9183 5 Mayt^XBotuyan, M.V. Toy-Palmer, A. Chung, J. Blake, R.C., II Beroza, P. Case, D.A. Dyson, H.J. 1996NMR structure of Cu(I) rusticyanin from Thiobacillus ferrooxidans: structural basis for the extreme acid stability and redox potential. ( A  263752-767"Journal of Molecular Biology SJESJEF@Bouchard, M. Benjamin, D.R. Tito, P. Robinson, C.V. Dobson, C.M. 2000Solvent effects on the conformation of the trransmembrane peptide gramicidin A: insights from electrospray ionization mass spectrometry.Biophysical Journal78 1010-1017  SJE 730>8Boucher, W. Laue, E.D. Campbellburk, S.L. Domaille, P.J. 1992tn2D 4D-NMR BACKBONE NUCLEI C-H-RAS P21 ISOTOPIC LABELLING LARGER PROTEINS NMR RESONANCE ASSIGNMENT SPECTROSCOPYf`Improved 4D-NMR Experiments for the Assignment of Backbone Nuclei in C-13/N-15 Labelled Proteins"Journal of Biomolecular NMR2 6 631-637t Nov 729<6Boucher, W. Laue, E.D. Campbellburk, S. Domaille, P.J. 19926/2D H 1 NMR HUMAN UBIQUITIN SPECTRA SPECTROSCOPYpj4-Dimensional Heteronuclear Triple Resonance NMR Methods for the Assignment of Backbone Nuclei in Proteins.(Journal of the American Chemical Society 1146a 2262-2264a 11 Mar 731RLBouhss, A. Krin, E. Munier, H. Gilles, A.M. Danchin, A. Glaser, P. Barzu, O. 1993CONFORMATIONAL CHANGE CONTAINS DOMAIN ESCHERICHIA-COLI IDENTIFICATION LIGHT-CHAIN KINASE PHOSPHORYLASE-KINASE PROTEINS SEQUENCE SKELETAL-MUSCLE ngCooperative Phenomena in Binding and Activation of Bordetella-Pertussis Adenylate Cyclase by Calmodulino&Journal of Biological Chemistryt 26833 1690-1694 25 Jan)4-:)./7L3 L 1617F@De Cock, H. Meeldijk, J. Overduin, P. Verkleij, A. Tommassen, J. 198960ESCHERICHIA LIPID MEMBRANE MUTATION PROTEIN SECAIn E. coli K-12, temp.-sensitive mutations in the secA gene have been shown to interfere with protein export. The effect of a secA mutation was strongly pleiotropic on membrane biogenesis. Freeze-fracture expts. as well as cryosections of the cells revealed the appearance of intracytoplasmic membranes upon induction of the SecA phenotype. The permeability barrier of the outer membrane to detergents was lost. Two alterations in the outer membrane may be responsible for this effect, namely the reduced amts. of outer membrane proteins, or the redn. of the length of the core oligosaccharide of the lipopolysaccharide, which was obsd. in phage-sensitivity expts. and by SDS-PAGE. Phospholipid anal. of the secA mutant, grown under restrictive conditions, revealed a lower content of the neg. charged phospholipid cardiolipin and of 18:1 fatty acid compared to those of the parental strain grown under identical conditions. These results are in line with the hypothesis that protein export and lipid metab. are coupled. 0006-3002JCMembrane biogenesis in Escherichia coli: effects of a secA mutation$Biochimica et Biophysica Acta 9853313-319Utrecht 3584, Neth.4-de Crouy-Chanel, A. Kohiyama, M. Richarme, G. 1996f`Specificity of DnaK for arginine/lysine and effect of DnaJ on the amino acid specificity of DnaK J Biol Chem 271R26 15486-15490 8663088XRhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=8663088'lfBiochimie Genetique, Institut Jacques Monod, Universite Paris 7, 2 Place Jussieu, 75005 Paris, France.\Ude Gier, J.W.L. Mansournia, P. Valent, Q.A. Phillips, G.J. Luirink, J. von Heijne, G. 1996nAssembly of a cytoplasmic membrane protein in Escherichia coli is dependent on the signal recognition particle . ?  FEBS Letters 399d3307-309 6/De Gier, JW Valent, QA Von Heijne, G Luirink, J 1997x3The E. coli SRP: preferences of a targeting factor.     FEBS Letters  NETHERLANDS 4081 1-4 0014-579397324087zBacterial Proteins Escherichia coli Eukaryotic Cells Membrane Proteins Signal Recognition Particle Support, Non-U.S. Gov'tResearch on the targeting of proteins to the cytoplasmic membrane of E. coli has mainly focused on the so-called 'general secretory pathway' (GSP) which involves the Sec-proteins. Recently, evidence has been obtained for an alternative targeting pathway in E. coli which involves the signal recognition particle (SRP). The constituents of this SRP pathway in E. coli are homologous to those of the well-characterized eukaryotic SRP pathway, which is the main targeting pathway for both proteins translocated across and inserted into the endoplasmic reticulum membrane. However, until recently, no clear function could be assigned to the SRP in E. coli. New studies point to an important role of the E. coli SRP in the assembly of inner membrane proteins.ZSJLF Department of Biochemistry, Arrhenius Laboratory, Stockholm University, Sweden. 2+de Groot, B.L. Vriend, G. Berendsen, H.J.C. 1999b[Conformational changes in the chaperonin GroEL: new insights into the allosteric mechanism."Journal of Molecular Biology 286 1241-1249  SJEd\UDe Guzman, R. N. Wu, Z. R. Stalling, C. C. Pappalardo, L. Borer, P. N. Summers, N. F. 1998VStructure of the HIV-1 nucleocapsid protein bound to the SL3 y-RNA recognition element = > Scienceo 279h 5439 384 - 388e3PRotein33333!3#3$3&333'3(3+303:39383;3<3B3G33P3O3L3M3R233e3b3_3[3Z3g3m3q3k3j3p/3{3}3~3333333333333333331'And1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a2w'a2z'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'aT* SarcoPlasmico k < k  k k k* k kX k k  f < f' f  f f? f f f f f f fl f f f!  f% f% f6sineg8 f 'fatig$Oggen*Rntkk!k4jinski kar o o1oosylmmaj!Ct EESIN4j'tjoreellio ssvasrss8er8Ms4'SabeGkKkgawa}0"hara5Mi8i3i3[kawai?i?i f' f  f f? f f f f f f fl f f f ! f% f% f' fatigO$ggenR*ntkk!kj4inski kar o o1oosylmmajC!t EESINjtorellio ssvasrsssabekGkKkgawa}"0hara3i[3kawai?ilz,+1L&0aLIyer, K.S. Klee, W.A. 1973ZSDirect spectrophotometric measurement of the rate of reduction of disulphide bonds. 2482707-710?The reactivity of the disulphide bonds of bovine a-lactalbumin. 1 3 &Journal of Biological Chemistry  3484@:Izadyar, L. Friboulet, A. Remy, M.H. Roseto, A. Thomas, D. 1993CATALYTIC ANTIBODIESMonoclonal Anti-Idiotypic Antibodies as Functional Intermal Images of Enzyme Active Sites: Production of a Catalytic Antibody with a Cholinesterase Activity9019 8876-8880VOProceedings of the National Academy of Sciences of the United States of American Izard, J.W. Kendall, D.A. 1994@9Signal peptides: exquisitely designed transport promoterspMolecular Microbiology135y765-773 SSG3,%Izard, J.W. Rusch, S.L. Kendall, D.A.n 1996~xThe amino-terminal charge and core region hydrophobicity interdependently contribute to the function of signal sequences 271i35 21579-215823&Journal of Biological Chemistry 34856/Izumi, Y. Wakita, M. Yoshino, H. Matsushima, N.r 1992AMPHIPHILIC PEPTIDES BINDING CALCIUM COMPLEX-FORMATION CONFORMATIONAL CHANGE LIGHT-CHAIN KINASE MELITTIN RESONANCE TROPONIN-C TRYPTIC FRAGMENTSPStructure of the Proteolytic Fragment F34 of Calmodulin in the Absence and Presence of Mastoparan as Revealed by Solution X-Ray Scattering Biochemistry3148 12266-12271 8 Dec 3486*#Izumiya, N. Noda, K. Anfinsen, C.B. 1971Synthesis of phenylalanyl-arginyl-leucyl-aspartic acid: a model study of the coupling of arginine-terminal tryptic fragments of proteins.'Archives of Biochemistry and Biophysics 144t1237-244 MayoD>J Biol ChemShi, Z. Krantz, B. A. Kallenbach, N. Sosnick, T. R. 2002ZTContribution of hydrogen bonding to protein stability estimated from isotope effects Biochemistry4172120-9.11841202 JAHZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11841202 34884-Jaattela, M. Wissing, D. Bauer, P.A. Li, G.C.7 1992ANTISENSE CYTO-TOXICITY EFFECTOR MOLECULE EXPRESSION FACTOR-ALPHA GAMMA-INTERFERON GENES GROWTH HEAT-SHOCK PROTEIN MANGANOUS SUPEROXIDE-DISMUTASE MOLECULAR-CLONING RESISTANCE TNF-ALPHA TUMOR NECROSIS FACTORb[Major Heat Shock Protein hsp70 Protects Tumor Cells from Tumor Necrosis Factor CytotoxicityN EMBO Journal1110 3507-35120 Oct 3487Jaattela, M. Wissig, D. 1992B12?12B12@12C12D12E12I12H12G12F12J12K12N12M12L12P12Q12R12T12S12V12X12Z12Y12[12\12]12_12^12`12a12b12d12c12e12f12f12f12f12f12f1ssage to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... % m@  (a @ s<  %% ` = HH=8BIM=Grphbj ==HH ==@b !!&+28Hydrogen exchange and the dynamic structure of proteins.48135-160*#Molecular and Cellular Biochemistryn20033/654636)8885445858585858585858585858585959 59 5959!59"59%59)59-59.59/59059+59@59A59B59C59D59N59O59P59R59,59S59T59`5'35+5_55+?57h494\4#49:59E69Q69Y69_69a69b69f69X69j69k6!6]6#0616670336^955519621/6897320737-2 1_0/60v1264545S/56/65v57P8102S/390/95718b9)7275395/96756828)77/19496`6/1071S/8836K31176537 /8640 c66/1071S/883K631176537 /8640c 66ALLylm6m83aminogeldanamycin.m/e.e2e2e4e2e6e6e7e*eidar!rse"g[greno,2lof. ogt st0oooOo?oRn&nnnnn nonn#^n'Qn#Ln+sn5n6n6)n63n6Cn6un6n7n8n8n^nemri' ylglycinetobeidin ee-g-gyl*m6m83aminogeldanamycin.m/e.e2e2e4e2e6e6e7e*eidar!rse"g[greno,2lof. ogt st0oooOo?oRn&nnnnn nonn#^n'Qn#Ln+sn5n6n6)n63n6Cn6cn6un6n7n8n8n^nemri' ylglycinetobeidin ee-gse4410 11R'63'141'15'16D'1$12) 23 352'94M56 627576N888$925d'5o2'>3p11 >1*Q1 1{1100+<08A000) 122M2531:'71]'33'34'336N45?56}677!8?9"33L54`4&4 4f4]7030"o0$N0+000500 0#1 INteractions VI VK V( Vx Vz V V V V V V V VH Vt V V V V V V L V } V  V  V  V  V  V* V  V![ V! 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Oas19954 Oas1995 Oas1996, Oas1996& Oas1997( Oas1997* Oas1998* Oas1998, Oas199824 Oas20000 Oas200125 Oas20014 Oas20013 Oas200270 Oas2002 Oates1993m Obar1990v& Obar19919 z Obar1991kC Obata1993$z Oberg19917- Oberg1994( Oberg1997- Oberhauser1999. Oberhauser1999n Oberholzer1993 $ Oberkanins1991p Oberman19922Obermann1998D2Obermann1998D8X Obita2003o Oblattmontal1993q Oblong1992 p Oblong1992 r Oblong1993  Obrien19929~ Obrien19929% Obrien1993 s Obrien1993 8v Obrink2002203Obukhova19919h Ocallaghan1992 & Ockner1983 r Ockner19844 Oconnor19929 Oconnor1992 Oda1992 Oda1992{ Oda1993z Oda19937 Oda1994-4 Oda1996| Odaka1992"Y Odaka1992 Odani1993P Oday199333 Odefey1995Y Odefey1996 8 Odent2003"  Odintsova1982x Odoevskaya1992 } Odom1990v Odom19919 Odom19929 Odom19929 Nutkins1990 Nutt1969 Nutt1992g Nutt19929j Nyberg1988k Nyberg1989  Nyberg1989O Nye1987 Nygard1991  Nyholm19929a Nyholm1993 +$ Nymeyer1998b Nystrom1992Z O'Donnell1990c O'Donohue1994#y O'Keefe1990e O'Neil1987 f O'Neil1989 'M O'Neil1990  O'Neil1995 * O'Neil1997 g O'Shea1989 i O'Shea1991 # Oakley19929j Oakley1992 l Oas1988$ Oas1992 Oas1996& Oas1997( Oas1997* Oas1998* Oas1998 Oates1993m Obar1990v& Obar19919 z Obar1991kC Obata1993$z Oberg1991( Oberg1997n Oberholzer1993 $ Oberkanins1991p Oberman1992o Oblattmontal1993q Oblong1992 p Oblong1992 r Oblong1993  Obrien19929~ Obrien19929% Obrien1993 s Obrien1993 h Ocallaghan1992 & Ockner1983 wOconnell1993vOconnell1993uOconnell1993tOconnell1993 Oconnor19929 Oconnor1992y Oconnor1993x Oconnor1993 Oda1992 Oda1992{ Oda1993z Oda19937 Oda1994| Odaka1992"Y Odaka1992 Odani1993P Oday19933 Odefey1996 "  Odintsova1982x Odoevskaya1992 } Odom1990v Odom19919 Odom19929 Odom19929 ` t   D  (!Goto, Y. Takahashi, N. Fink, A.L.u 19904-Mechanism of acid-induced folding of proteins Biochemistry2914 3480-34884 10 Apr 2741 JAH 2735Goto, Y. Fink, A.L. 1990$MOLTEN-GLOBULE STATE PROTEINSfD>Phase Diagram for Acidic Conformational States of Apomyoglobin 2144803-8055 20 Aug"Journal of Molecular Biology 2740&Goto, Y. Okamura, N. Aimoto, S.c 19914-ADENYLATE KINASE COMPLEX MOLTEN-GLOBULE STATEBB;ATP-Induced Conformational Transition of Denatured ProteinsAJournal of BiochemistryM 1095N746-750M May 2739Goto, Y. Nishikiori, S. 1991ACETYLATION OF AMINO GROUPS APOMYOGLOBIN CONFORMATIONAL STATES CONSTANT FRAGMENT CYTOCHROME-C ELECTROSTATIC INTERACTION FERRICYTOCHROME-C HYDROGEN-EXCHANGE IMMUNOGLOBULIN LIGHT CHAIN MASS-SPECTROMETRY MOLTEN GLOBULE NMR PROTEIN PROTEIN FOLDING STRUCTURAL CHARACTERIZATIONRLRole of Electrostatic Repulsion in the Acidic Molten Globule of Cytochrome-c 2223679-686 5 Dec-"Journal of Molecular Biology 2732Goto, Y. Aimoto, S. 1991$MOLTEN-GLOBULE STATE PROTEINS TNAnion and pH-Dependent Conformational Transition of an Amphiphilic Polypeptide 2182i387-396i 20 Mar"Journal of Molecular BiologyGoto, Y. Nishikiori, S. 1992MRole of electrostatic repulsion in the acidic molten globule of cytochrome c.  K L  222679-686"Journal of Molecular Biology 2736Goto, Y. Hagihara, Y. 1992AGGREGATION AQUEOUS MELITTIN HIGH-RESOLUTION H-1-NMR MODEL MOLTEN-GLOBULE STATE MONOMERIC MELITTIN PEPTIDES PROTEINS SELF-ASSOCIATION STABILIZATIONP<6Mechanism of the Conformational Transition of Melittin Biochemistry313732-738 28 Jan 2730Goto, Y. 1992haDisulfide bond formation in proteins and protein folding--crisis of Creighton's model. [Japanese]375880-885 AprN@:Tanpakushitsu Kakusan Koso (Protein, Nucleic Acid, Enzyme) 2737>7Goto, Y. Hagihara, Y. Hamada, D. Hoshino, M. Nishii, I. 1993COLD DENATURATION COMPACT CONFORMATIONAL TRANSITION FERRICYTOCHROME-C FOLDED APOMYOGLOBIN INTERMEDIATE MOLTEN-GLOBULE STATE NMR PROTEIN STABILITY STAPHYLOCOCCAL NUCLEASErleAcid-Induced Unfolding and Refolding Transitions of Cytochrome-c - A 3-State Mechanism in H2O and D2O Biochemistry3244 11878-11885 9 NovGoto, Y. 1993ZSProtein folding--conformation and stability of the molten globule state. [Japanese]:3Seikagaku (Journal of Japanese Biochemical Society)655321-337 May 2731 27294-Goto, S. Korematsu, K. Nagahiro, S. Ushio, Y.e 1993CHOLINE ACETYLTRANSFERASE DENSITY DISEASE EXPRESSION IDENTIFICATION IMMUNOFLUORESCENCE IMMUNOPEROXIDASE IMMUNOREACTIVITY NEOSTRIATUM POSTNATAL-DEVELOPMENT STRIATUM SYNAPTIC VESICLE MEMBRANE SYNAPTOPHYSIN (PROTEIN-P38)IxrDistinct Neuronal Subset Reveals Perikaryal Immunostaining for Synaptophysin (Protein-p38) in the Striatum of RatsActa Neuropathologica 863302-305 Aug6>7Goto, Y. Hagihara, Y. Hamada, D. Hoshino, M. Nishii, I. 1993iAcid-induced unfolding and refolding transitions of cytochrome c: a three-state mechanism in H2O and D2O. ? @ ^ @_ f @g  Biochemistry32 11878-11885@ 273882Goto, Y. Kogure, E. Takagi, T. Aimoto, S. Aoba, T. 1993HBBOVINE TOOTH ENAMEL CIRCULAR-DICHROISM MINERAL INTERACTION PROTEIN}Molecular Conformation of Porcine Amelogenin in Solution - 3 Folding Units at the N-Terminal, Central, and C-Terminal RegionseJournal of Biochemistryf 11331 55-60  Jan2 H G F E@1@ Df C< B A @ ? 2428F@Gadella, T.W.J. Bastiaens, P.I.H. Visser, A.J.W.G. Wirtz, K.W.A. 1991BOVINE LIVER CONVOLUTION METHOD LABELED PHOSPHATIDYLCHOLINE LEYDIG-CELLS PHOSPHATIDYLCHOLINE-TRANSFER PROTEIN PHOSPHATIDYLINOSITOL TRANSFER PROTEIN PHOSPHOLIPID TRANSFER PROTEINS PURIFICATION RAT-LIVER ROTATIONAL-DYNAMICSuShape and Lipid-Binding Site of the Nonspecific Lipid-Transfer Protein (Sterol Carrier Protein-2) - A Steady-State and Time-Resolved Fluorescence Study Biochemistry3022 5555-55642 4 Jun5 2429@9Gaestel, M. Benndorf, R. Hayess, K. Priemer, E. Engel, K. 1992ALPHA CALCINEURIN CATALYTIC SUBUNIT CELLS EHRLICH ASCITES TUMOR MOLECULAR-CLONING PHOSPHORYLATION STRESS PROTEINS SUBSTRATE-SPECIFICITY TUMOR NECROSIS FACTOR|uDephosphorylation of the Small Heat Shock Protein hsp25 by Calcium Calmodulin-Dependent (Type-2B) Protein Phosphatase&Journal of Biological Chemistry 26730 21607-21611 25 Oct 2430:4Gaffney, D. Freeman, D.J. Shepherd, J. Packard, C.J. 1993APOLIPOPROTEIN-B ATHEROSCLEROSIS CHOLESTEROL LEVELS DNA POLYMORPHISM FAMILIAL DEFECTIVE APOLIPOPROTEIN-B-100 GENE INDIVIDUALS INSERTION-DELETION POLYMORPHISM LOW-DENSITY LIPOPROTEIN MUTATION POPULATION SERUM-CHOLESTEROL SIGNAL-SEQUENCE leThe ins/del Polymorphism in the Signal Sequence of Apolipoprotein-B Has No Effect on Lipid ParametersClinica Chimica Acta 2182131-138 30 Sep 2431.(Gaigg, B. Lafer, G. Paltauf, F. Daum, G. 1993BOVINE BRAIN CYTOSOL FLUORESCENT PHOSPHOLIPID PHOSPHATIDYLETHANOLAMINE PHOSPHATIDYLINOSITOL TRANSFER PROTEIN PHOSPHATIDYLSERINE PHOSPHOLIPID-TRANSFER PROTEIN S-CEREVISIAE SACCHAROMYCES-CEREVISIAE SPECIFICITY TRANSFER PROTEIN YEASTleInteraction of the Yeast Phosphatidylserine Transfer Protein with Artificial and Biological Membranes $Biochimica et Biophysica Acta 11462 301-3040 14 Marf_Gainutdinov, M.K. Konov, V.V. Ishmukhamedov, R.N. Zakharova, T.N. Khalilova, M.A. Safarov, K.S. 1992Effective Pore Diameter in the Inner Membrane of Rat Liver Mitochondria and Selectivity of Monovalent Cation Transport Induced by Submicromolar Concentrations of Ca2+ or A23187 and EDTABiochemistry - USSR 5711 1120-1126  Novd 2432BUTYRATE CA-2+-DEPENDENT PORE CA2 CALCIUM-TRANSPORT CYCLOSPORIN-SENSITIVE PORE CYCLOSPORINE HEART-MITOCHONDRIA INHIBITION INVITRO MAMMALIAN MITOCHONDRIA MITOCHONDRIA OXIDATIVE STRESS 2433$Gairin, J.E. Oldstone, M.B.A.i 1993TNANTIGENS BINDING CELLS CHORIOMENINGITIS CONFORMATION MHC MOLECULES RECOGNITIONVirus and Cytotoxic T-Lymphocytes - Crucial Role of Viral Peptide Secondary Structure in Major Histocompatibility Complex Class-I InteractionsJournal of Virology675 2903-2907 May*$Galani, D. Fersht, A. R. Perrett, S. 2002haFolding of the yeast prion protein Ure2: kinetic evidence for folding and unfolding intermediates} J Mol Biol 3152r213-27.d11779240 JAHmZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11779240i 2434,%Galanis, M. Devenish, R.J. Nagley, P. 1991PIATP SYNTHASE COMPLEX GENES INVITRO ORGANELLE SUBUNIT-8 YEAST MITOCHONDRIASpiDuplication of Leader Sequence for Protein Targeting to Mitochondria Leads to Increased Import Efficiencyr FEBS Letters 282t2425-430V 6 May60Galanis, M. Wang, L.F. Nagley, P. Devenish, R.J. 1993Duplication of Secretion Signal Sequences Is Deleterious for the Secretion of Human Interferon-alpha-4 from Saccharomyces-Cerevisiae and Bacillus-Subtilis302271-282 Jun 2435d^ALPHA ESCHERICHIA-COLI EXPRESSION GENE INVIVO MEMBRANE MITOCHONDRIA MUTANT NUCLEOTIDE-SEQUENCE60Biochemistry and Molecular Biology International 243660Galat, A. Creighton, T.E. Lord, R.C. Blout, E.R. 1981rkCircular dichroism, Raman spectroscopy, and gel filtration of trapped folding intermediates of ribonucleaseN Biochemistry203s594-601f 3 Feb Galat, A. 1985tmTime scale, geometrical constraints, and disulphide bond formation in the folding of small globular proteins. Biopolymers24279-285.67 31 284M5= 1998 Dec 18Modulation of intrinsic phi,psi propensiti98783731 284M5= 1998 Dec 18Modulation of intrinsic phi,psi propensities of amino acids by neighbouring residues in the coil regions of protein structures: NMR analysis and dissection of a beta-hairpin peptidel1597-609Analysis of residues in coil regions of protein structures presents a novel approach to deconvoluting the various competing factors which determine the intrinsic phi,psi propensities of amino acids free from the regular interactions associated with beta-strands and alpha-helices. We have considered the role of context on phi,psi preferences by examining the effects of neighbouring residues in modulating coil propensities within a data base of 512 high-resolution, low-homology structures. In the general case, when flanking residues are beta-branched or aromatic (Val, Ile, Tyr and Phe) the beta-propensity (Pbeta) increases significantly, largely due to steric effects between flanking residues. More subtle residue-specific effects are apparant when Pbeta values are examined in detail, showing "random coil" conformations to be highly sequence-dependent. The effects of flanking residues on phi distributions have been used to calculate context-dependent average 3JNH-Halpha coupling constants. We have examined these findings in the context of the folding of a model 16-residue beta-hairpin peptide, "mutant" hairpin (VSI-->KSK sequence change) and the isolated C-terminal beta-strand fragments of both hairpins. We find a better correlation between 3JNH-Halpha values derived from the data base model and those determined experimentally when context-dependent phi distributions are considered. The individual C-terminal beta-strand sequences (GKKITVSI versus GKKITKSK) of the two hairpins are predisposed to different extents to formation of an extended beta-like conformation. Conformational "predisposition" in this context may contribute significantly to beta-hairpin stability.'RKDepartment of Chemistry, University of Nottingham, Nottingham, NG7 2RD, UK.iHBGriffiths-Jones, S. R. Sharman, G. J. Maynard, A. J. Searle, M. S.("99096890 0022-2836 Journal Article J Mol BiolAmino Acid Sequence Amino Acids/*chemistry Magnetic Resonance Spectroscopy *Models, Molecular Molecular Sequence Data Peptides/chemistry Protein Conformation Protein Folding Protein Structure, Secondary Proteins/*chemistry Support, Non-U.S. Gov't Waterjdhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=987837360Griffiths-Jones, S.R. Maynard, A.J. Searle, M.S. 19990Dissecting the stability of a b-hairpin peptide that folds in water: NMR and molecular dynamics analysis of the b-turn and b-strand contributions to folding   p q { | "Journal of Molecular Biology 292 1051-1069 JAH/U/1/1/1/1/1/1/1/1/1/1)/11+ 11/1/1/1/1213&1/14x1414141414y14z14{14|14}1414141414141414t1'Z1/151515151515151515151515161616161616 16 16 16161FFOLDING PROTEIN SIMIAN VIRUS-40 SUBUNIT TAIL SPIKE PROTEINrlTemperature-Sensitive Mutations in the Phage-P22 Coat Protein Which Interfere with Polypeptide Chain Folding&Journal of Biological Chemistryh 268i13 9358-9368 5 May 27144.Gordon, C.L. Sather, S.K. Casjens, S. King, J. 1994rkSelective in vivo Rescue by GroEL/ES of Thermolabile Folding Intermediates to Phage P22 Structural ProteinsU&Journal of Biological Chemistryl 269n 27941-279512Vfoldingr*erNrrr rr+BrUr r(r, r, r)r,r<r#<r;rFrr,r)r,r+Fr+r,r,r,r+r+r,rr*pr(r*r)r+r* r+r+r,$r,%r,&r,*r)r,/r,7r,:rr{r{r{r{r{r{r{r{r{r{r{r{r{r6[>6ZB.K. Wittebort, R.J. Ramamoorthy, A.\ 1998Characterization of (15)N chemical shift and (1)H-(15)N dipola Lee, D.K. Ramamoorthy, A. 1998pjDetermination of the solid-state conformations of polyalanine using magic-angle spinning NMR spectroscropy$Journal of Physical Chemistry 1030271-275 Dec 15^XConformations of the powder ssamples of poly-L-alanine with molecular weights of 356 Da 15000 Da (PLA-200) and 23 600 Da (PLA-333) were characterized by (13) C cross-polarization magic-angle spinning (CPMAS) and (1)H combined rotation and multiple pulse (CRAMPS) solid-state NMR spectroscropy. From the (13) C and (1)H isotropic chemical shift values, it is predicted that hte main chain conformations of tetraalanine and PLA-200 are mainly beta-sheet while the conformation of PLA-333 is mainly an alpha-helix. It is unusual and interesting that a high moleuclar weight homopolypeptide, PLA-200, has a beta-sheet conformation rather than an alpha-helix conformation. The effect of dichloroacetic acid solvent on the backbone conformation of these peptides was also studied. It is inferred from solid state NMR results that conformations of tetralaanine and PLA-333 are similar before and after crystallization from DCA. On the other hand, the backbone conformation of PLA-200 is 60% alpha-helix and 40% beta-sheet after crystallization from the DCA solvent. Variable temperature studies are also reported.0)Lee, D.K. Wittebort, R.J. Ramamoorthy, A.\ 1998Characterization of (15)N chemical shift and (1)H-(15)N dipolar coupling interactions in a peptide bond of uniaxially oriented and polycrystalline samples by one-dimensional dipolar chemical shift solid-state NMR spectroscopym.(Journal of the American Chemical Society 120e 8868-8874t May 7 S0002-7863(98)@9The magnitudes and orientations of the principal elements of the (15)N chemical shift and (1)H-(15)N dipolar coupling interaction tensors pertaining to the glycine residue in (15)N-acetyl glycine (NAG) and [(15)N-Gly] collagen were determined by the analysis of one-dimensional dipolar chemical shift powder patterns. A one-dimensional (1)H-(15)N dipolar (15)N chemical shift spectrum was obtained on a [(15)N-Gly]collagen fiber sample with the giver axis oriented parallel to the external magnetic field. The dipolar chemical shift spectrum enabled the orientation of the peptide plane to be determined relative to the direction of the applied magnetic field or the triple-helix axis of the collagen fiber. The magnitudes of the principal elements fo the tensors and their orientations in teh molecular frame for these sites are quite different. The magnitudes for the chemical shift tensors are 42.3, 67 and 223.4 ppm for [(15)N-Gly]collagen and 37,82.8, and 220.4 ppm for NAG. The angle (betaN) betwen the least shielded (15)N chemical shift tnesor element, alpha 33N and the N-H bond is 24.5 degrees for NAG. The angle (alphaN) between teh most shielded (15)N chemical shift tensor elemetn and the projection of the N-H bond on the plane is 145 degrees for [(15)N-Gly]collagen and 25 degrees for NAG. Because of the identical dipolar chemical shift powder patterns for four different alphaN values (35, 145, 215, and 325 degrees) the correct value of the alphaN angle was determined as 145 degrees using the dipolar chemical shift spectrum of the oriented [15N-Gly]collagen sample.'rkBiophysics Research Division and Dept. of Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055t7LAtT7Pa7^a7_a7`a7da7ea7fa7ga7ha7ia7la7ma7qa7ta7va7wa7{a7}a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a8a8a8a8a8 a8a6a8*a8.a85a88a8:a8;a8=a8Ia8La8Na8Ra8Ta8[a8da8fa8ga8ia8la8na8oa8ta8va8wa8ya8{a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a8a6a8a8a)&a)+a)*a)a'Sa1J'a1f'a1'a1'a1'a1'a1'a1'a+)a*)a)aS'aJ1'af1'a1'a0ofc0n0n0R0000n0n0n0n0R00n0n0n0n1n#n#nn)/1nn0n0n=n0n+ nzn0n0n4)n4n&n4n'Zn52n585n5n5n5n55n5n5n5n5n5n5n5n5n5R6R6R6i6i666 n6 n6 n6 n5 Inm5c5c(c50c56c59c5:c5<c5;c5>c5Bc5Ec5Ic5Jc5Lc5Oc5Nc5Qc5Sc5Yc5]c5\c5[c5dc5cc5`c5_c5hc5gc5fc5wc5vc5uc5c5c5c5c5c5c5c5c5c1c5c5c/c-8c5c5c5c5c5c5c5c5c5c5c5c5c5c5c5c5c4'And4'a4'a4s'a4'a4'a4'a4'a4'a4'a4'a4'a5:'a5E'a5G'a5I'a5H'a5K'a5J'a5L'a5P'a5O'a5Y'a5]'a5d'a5b'a5a'a5i'a5h'a5f'a5m'a5p'a5o'a5s'a5y'a5'a5'a5}'a5|'a5{'a5'a5'a5'a5'a5'a5'a5'a1'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'a5'aTHIsR+os+psos)2s+rs'Qs'Ms+ws+ys+{s+~sOss!;s).sss+s+s+ts+Ys+ss0s0s0s0s0s0s0s0s0s0s)/s1s0s=s0s+ szs&s'Zs52s58s5s5s5s5s6s6s6 s6 s6 s6s6s6s6s6s6s6s6s6s6s6sSpinachULiLLL L L LL9LL5LLLrLsL9L L!EL#L$L%L#L8L=LOL$KIA lDDD @dddd dd 1dle lluljlSlss~yNNNNmN N xk"Mk$k$k"Mk Bk Lningy"y6Zy7y Syygard, P.O. Kihlgren, A. Svensson, M. Carlsson, U. 1993ALPHA-LACTALBUMIN CIRCULAR-DICHROISM FOLDED APOMYOGLOBIN INTERMEDIATE GUANIDINE-HYDROCHLORIDE DENATURATION MOLTEN-GLOBULE STATE PROTEIN STABILITY UREACharacterization of Folding Intermediates of Human Carbonic Anhydrase .2. Probing Substructure by Chemical Labeling of SH Groups Introduced by Site-Directed Mutagenesis Biochemistry321y224-231 12 Jan Martin, J. 1991 Nature 352  36-42Tl\  367681Juretic, D. Lee, B. Trinajstic, N. Williams, R.W.f 1993ALPHA-HELICES AMINO-ACID SEQUENCE ESCHERICHIA-COLI GLOBULAR-PROTEINS NEURAL NETWORKS PARAMETERS PHOTOSYNTHETIC REACTION CENTER RHODOBACTER-SPHAEROIDES R-26 RHODOPSEUDOMONAS-VIRIDIS SECONDARY STRUCTURE PREDICTIONtf_A suite of FORTRAN programs, PREF, is described for calculating preference functions from the data base of known protein structures and for comparing smoothed profiles of sequence-dependent preferences in proteins of unknown structure. Amino acid preferences for a secondary structure are considered as functions of a sequence environment. Sequence environment of amino acid residue in a protein is defined as an average over some physical, chemical, or statistical property of its primary structure neighbors. The frequency distribution of sequence environments in the data base of soluble protein structures is approximately normal for each amino acid type of known secondary conformation. An analytical expression for the dependence of preferences on sequence environment is obtained after each frequency distribution is replaced by corresponding Gaussian function. The preference for the alpha-helical conformation increases for each amino acid type with the increase of sequence environment of buried solvent accessible surface areas. We show that a set of preference functions based on buried surface area is useful for predicting folding motifs in alpha-class proteins and in integral membrane proteins. The prediction accuracy for helical residues is 79% for 5 integral membrane proteins and 74% for 11 alpha-class soluble proteins. Most residues found in transmembrane segments of membrane proteins with known alpha-helical structure are predicted to be indeed in the helical conformation because of very high middle helix preferences. Both extramembrane and transmembrane helices in the photosynthetic reaction center M and L subunits are correctly predicted. We point out in the discussion that our method of conformational preference functions can identify what physical properties of the amino acids are important in the formation of particular secondary structure elements.uVOConformational Preference Functions for Predicting Helices in Membrane Proteinsa Biopolymersb332255-273 Feb3 3677<6Jurivich, D.A. Sistonen, L. Kroes, R.A. Morimoto, R.I. 1992ACTIVATION AMINO ACID ANALOGS ASPIRIN-LIKE DRUGS DNA-BINDING EXPRESSION HUMAN-CELLS INHIBITION PROTEIN SEQUENCE TRANSCRIPTION FACTORB ? :$ ; < 9 6 7 2192$Fersht, A.R. Knill-Jones, J.W. 1983yContribution of 3' leads to 5' exonuclease activity of DNA polymerase III holoenzyme from Escherichia coli to specificityo 1654c669-682 25 Apr"Journal of Molecular Biology 2191$Fersht, A.R. Knill-Jones, J.W. 1983PJFidelity of replication of bacteriophage phi X174 DNA in vitro and in vivo 1654.633-654t 25 Apr"Journal of Molecular Biology 2177 Fersht, A.R. 1984*$Fidelity of DNA replication in vitro 179525-5334-Advances in Experimental Medicine and Biology 2208 Fersht, A.R. Winter, G.P. 198560Redesigning enzymes by site-directed mutagenesis 111204-218i CIBA Foundation Symposiumi 220782Fersht, A.R. Wilkinson, A.J. Carter, P. Winter, G. 1985^WFine structure-activity analysis of mutations at position 51 of tyrosyl-tRNA synthetase Biochemistry2421 5858-58612 8 Oct 2202~wFersht, A.R. Shi, J.P. Knill-Jones, J. Lowe, D.M. Wilkinson, A.J. Blow, D.M. Brick, P. Carter, P. Waye, M.M. Winter, G. 1985RKHydrogen bonding and biological specificity analysed by protein engineering Nature 314 6008235-2380 21-27 Mar0 21942,Fersht, A.R. Leatherbarrow, R.J. Wells, T.N. 1987~Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships Biochemistry2619 6030-6038N 22 Sep 2179 Fersht, A.R. 19872+Linear free energy relationships are valid:Protein Engineeringy1i6442-445 Deci 2178 Fersht, A.R. 1987jdDissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis Biochemistry2625 8031-8037 15 Dec 2193>7Fersht, A.R. Knill-Jones, J.W. Bedouelle, H. Winter, G.e 1988XR#AMINO ACID ACTIVATION. AMINO ACYL T RNA SYNTHETASES/ME [METABOLISM] ESCHERICHIA COLI/EN [ENZYMOLOGY]. ESCHERICHIA COLI/GE [GENETICS] #KINETICS. MATHEMATICS. MUTATION. PROTEIN CONFORMATION. SUPPORT #NON-U.S. GOV'T. THERMODYNAMICS. TYROSINE/ME [METABOLISM]. TYROSYL T #RNA SYNTHETASE/GE [GENETICS]. TYROSYL T RNA SYNTHETASE/ME [METABOLISM]Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanismR Biochemistry275  1581-1587u 8 Marf 2180 Fersht, A.R. 1988#BONDING. KINETICS. MODELS, THEORETICAL. MUTATION. PROTEIN BINDING #CALORIMETRY. ENZYMES/GE [GENETICS]. ENZYMES/ME [METABOLISM]. HYDROGEN SUPPORT, NON-U.S. GOV'T. THERMODYNAMICSIRelationships between apparent binding energies measured in site-directed mutagenesis experiments and energetics of binding and catalysisp Biochemistry275y 1577-1580y 8 Mar1 2205"Fersht, A.R. Sternberg, M.J. 1989jdCan a simple function for the dielectric response model electrostatic; effects in globular proteins?Protein Engineeringl27 527-530 May 2206Fersht, A.R. Wells, T.N. 1991f_Linear free energy relationships in enzyme binding interactions studied; by protein engineeringProtein Engineering43229-231 Feb TMFersht, A.R. Bycroft, M. Horovitz, A. Kellis, J.T. Matouschek, A. Serrano, L. 1991.(Pathway and stability of protein folding^XPhilosophical Transactions of the Royal Society of London. Series B: Biological Sciences 332 1263171-176\ 29 May 2185BARNASE BINDING-ENERGY CATALYSIS ENERGETICS INTERMEDIATE NMR RIBONUCLEASE SITE-DIRECTED MUTAGENESIS STATE TRANSFER RNA-SYNTHETASE JAHFersht, A. Winter, G. 1992Protein Engineering17292-294n$Trends in Biochemical SciencesZ "A6L%7`78681692S66S+6S9A+.r+r6r97r&rr hrmGC71A7A7A7A7'A2A3C6C6C6C6CC2FF83G#1lberseo$org(ten6m'mandrronson)S)s-Fserudb+*a/a0a3a3A445447X47q48:4342A3A gyans*ssstadotedurovzacccbbadim+r&rrh rmGC2A3C6C6C6C6CC2FF1#lberseo$org(ten6m'mandrronson)S)sF-serudb*+a/a0a3a3A44544342 3A gyans*ssstadotedurovzacccbbadimimadim~ kMet a wa#a=aaa waaaa)aa+la6 a8aaa aIa!5+s175171718I18|101'P467'P7!305"5!55!n70!n3+s6abb8booolics sr s s s6/ s6 s8 s  s  s  s7 a7 a8A a allys6 s:smH; H  H N H  H, Hj H H' H H%% H, H t H H H  TG a aIa!5s+101P'467P'7!305"5!55n!70n!3s+6abbboolics sr s s s  s  s  s ally:smt; H  HN  H  H, Hj H H' H H%% H, Ht  H H H ƴ TG l TUBERCULOSISr' U" U#^ U# U$? U$ U% U&- U6  U U U#^ O% O58 O6  O<OUS6NslinoiEUU!Uu%8ULAREE6>E6NEgEi i xiincccc,c?ccccjccccc c ccccc c c c #c bc 1c c ccccccccccccccc>cccacmcccccccccc@cAcc@c c xc c!c!2c#.c#Bc#c#c%c& c&2c&eccccccccccccc>cccacmccccccz, A. Kellis, J.T. Matouschek, A. Serrano, L. 1991.(Pathway and Stability of Protein Folding 332 1263171-176 29 May 2185BARNASE BINDING-ENERGY CATALYSIS ENERGETICS INTERMEDIATE NMR RIBONUCLEASE SITE-DIRECTED MUTAGENESIS STATE TRANSFER RNA-SYNTHETASE^XPhilosophical Transactions of the Royal Society of London. Series B: Biological SciencesFersht, A. Winter, G. 1992Protein Engineering17292-294n$Trends in Biochemical Sciences "ion. The procedure is applied here to the 22-residue peptide hormone motilin, and the results are compared to those obtained using the conventional method of analyzing mu 7360Smith, R.F. Smith, T.F. 1992ALIGNMENTS AMINO ACID SEQUENCES DISTANTLY RELATED PROTEINS GLOBULAR-PROTEINS HOMOLOGOUS PROTEINS HOMOLOGY IDENTIFICATION MODELLING PREDICTION PROFILE ANALYSIS PROTEIN SEQUENCE RECOGNITION SECONDARY STRUCTURE SIMILARITIES TREESPattern-Induced Multi-Sequence Alignment (PIMA) Algorithm Employing Secondary Structure-Dependent Gap Penalties for Use in Comparative Protein ModellingProtein EngineeringR5r1 35-41R Jan 7359:3Smith, R. Separovic, F. Bennett, F.C. Cornell, B.A. 1992ASSOCIATION BILAYER-MEMBRANES BIOLOGICAL-MEMBRANES CONFORMATION GRAMICIDIN-A NUCLEAR MAGNETIC-RESONANCE PHOSPHOLIPID MODEL MEMBRANES SPECTROSCOPY SPIN-LABELED MELITTIN SYNTHETIC MELITTINNGMelittin-Induced Changes in Lipid Multilayers - A Solid-State NMR StudyNBiophysical Journal 632E469-474 Aug 7354^WSmith, L.J. Redfield, C. Boyd, J. Lawrence, G.M. Edwards, R.G. Smith, R.A. Dobson, C.M. 1992RKHuman interleukin 4. The solution structure of a four-helix bundle; proteint 2244o899-904` 20 Apr"Journal of Molecular Biology 734982Smith, D.F. Stensgard, B.A. Welch, W.J. Toft, D.O. 199259-KILODALTON PROTEIN BINDING-PROTEIN CHICKEN OVIDUCT COMPLEX GLUCOCORTICOID RECEPTOR MOLYBDATE MONOCLONAL-ANTIBODIES RECONSTITUTION STEROID-RECEPTORS VIRUS TRANSFORMING PROTEINpjAssembly of Progesterone Receptor with Heat Shock Proteins and Receptor Activation Are ATP Mediated Events&Journal of Biological Chemistry 2672t 1350-1356t 15 Jan 7348*$Smith, D.E. Zhang, L. Haymet, A.D.J. 1992&HYDROPHOBIC INTERACTION SOLVENT`YEntropy of Association of Methane in Water - A New Molecular Dynamics Computer SimulationN.(Journal of the American Chemical Society 11414 5875-5876p 1 Jul 7343rlSmith, A.B. Keenan, T.P. Holcomb, R.C. Sprengeler, P.A. Guzman, M.C. Wood, J.L. Carroll, P.J. Hirschmann, R. 1992Design, Synthesis, and Crystal Structure of a Pyrrolinone-Based Peptidomimetic Possessing the Conformation of a beta-Strand - Potential Application to the Design of Novel Inhibitors of Proteolytic Enzymes.(Journal of the American Chemical Society 11426 10672-10674c 16 Dec"Smith, R.D. Light-Wahl, K.J. 1993The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: promise, pitfalls and prognosis"Biological Mass Spectrometry229 493-501 ESI-MS SJE6 7357<5Smith, L.J. Sutcliffe, M.J. Redfield, C. Dobson, C.M. 1993:43-DIMENSIONAL STRUCTURES CHEMICAL-SHIFTS COUPLING-CONSTANTS DISTANCE GEOMETRY EGG-WHITE LYSOZYME ENZYME LYSOZYME NMR-SPECTROSCOPY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE NUCLEAR OVERHAUSER EFFECT PANCREATIC TRYPSIN-INHIBITOR PROTEIN STRUCTURES PROTEIN-STRUCTURE SECONDARY STRUCTURE,%Structure of Hen Lysozyme in SolutionC 2294I930-944 20 Feb"Journal of Molecular Biology 7352Smith, J.L. Wright, P. 1993.(Biophysical Methods - Editorial Overview,%Current Opinion in Structural Biology@375723-724 Octy@9Smith, D.D. Boyd, K.G. Hopton, D. Baxter, R.L. Ramage, R. 1993Phosphorus-Based Reagents in Peptide Synthesis -Synthesis of Methionine-Enkephalin and the Solution Conformation of Its N-Diphenylphosphinoyl Derivative<5Journal of the Chemical Society - Perkin Transactions15551-556d 7 Mar 7347INCOMPLETE ENKEPHALIN ACIDS BETA-SHEET CRYSTAL-STRUCTURE FORM NUCLEAR MAGNETIC-RESONANCE RECEPTOR SOLID-PHASE SYNTHESIS SPECTROSCOPY X RAY DIFFRACTION t1976 6' 6F6!666{6z6 6d6666z6y6{666!66 6 6 66165Q6 62667`8 8L3 3 3333e333"3333*3)3:333 3!3$3%r3&&3)3)3*393/G3- 3-313@ AllicottiSUMI5gmannI'= OANTIGENS' p$ C.Mcatelli0 I0% I3 I3 IION/ D DETERMINANTSppeptide ROTEINi REACTIVITYn cognitionspecificbteric w'? w  w~ w w w wk w  w  w[ w w\ w w w` wb wc wH wz w} w/ w w%s w% w-: w-d w.m w/{ w. w1 w3 w3 w4q w5 w5 7 8 8 9Q  4200343434343435835:35<35;35=35>35?35A35B35E35G35F35I35H35K35J35O35S35U35T35Y35X35W35V35]35\35[35Z35^35d35c35b35l35k35j35i35h35g35f35m35q35p35o35r35z35y35x35w35v35v35v3v53v53v53v53v53v534 C4 A4 A4A4A4A4A4A4A4A4A4A4%A4+A4&A43A45A4HA41A4MA4PA4]A4[A4XA4gA4fA4eA4dA4cA4bA4nA4mA4lA4jA4A4wA4yA4zA4~A4A4A4A4)A4tA4A4A4A"AA)A4A1A3iA4AA4A4A4AA/A+A+A+A+AHe12840754072620345655"65"M6h660152668H3463B8E8087761B<6.B9i7702027513755257!8j6,053128567i3377i48F437266%36%68J58498I52678031799859/9/0k0,02"45523659741798D79118G8339 99!9"9(9/99=9 9 6_6 66$q6%1l118386 68859683869+96000&0 z0 y0000/00J0 h0 0 0!0-DOfc-En-Fn-Gn-In-Jn-Mn,n,n-Nn-;n-Tn-Vn-Wn-Xn-Yn-Zn-[n!n-`n-en-gn-hn-jn-kn-mn-nnn-n nn-n-n-n-n+n n ,nn n}n-n-n-n-n-n-n-n-n-n-n-n-n-n-n-n,n,n-On-OnO-n-On-On-On !,!:!,!!`!,..!n Tanford, C.a 1980The hydrophobic effect  New York, NY Jhon Wiley & Sonsl 7737Tang, W. Gilman, A.G. 1995IConstruction of a Soluble Adenylyl Cyclase Activated by Gsa and Forskolin 9 @: @< Science 268  1769-1772B(!Tang, W. Stanzel, M. Gilman, A.G. 1995B;Truncation and Alanine-Scanning Mutants of Adenylyl Cyclase Biochemistry34 14563-14572BF@Tang, K.S. Guralnick, B.J. Wang, W.K. Fersht, A.R. Itzhaki, L.S. 1999@:Stability and folding of the tumour suppressor protein p16"Journal of Molecular Biology 285 1869-1886JAH SJE 7739(!Tani, K. Tokuda, H. Mizushima, S., 1990ATP CONFORMATION CONTG DISULFIDE ESCHERICHIA FORCE MEMBRANE PREPROTEIN PROTEIN PROTONMOTIVE SECA SECRETORY TRANSLOCATION TRANSPORTIn the absence of .DELTA.~.mu.H+, the in vitro translocation of proOmpA resulted in the stable accumulation of a possible translocation intermediate in addn. to a transiently accumulating one. The stable intermediate was detected on a polyacrylamide gel as 2 proteinase K-resistant bands corresponding to a mol. wt. of .apprx.28,000. The appearance of the bands was appreciably enhanced when proOmpA was oxidized with ferricyanide. No mature OmpA appeared. When proOmpA reduced with dithiothreitol was used, on the other hand, the bands did not appear at all. Upon the replacement of cysteine-302 of OmpA with glycine, the intermediate accumulation was abolished. The proOmpA treated with dithiothreitol was labeled with N-[3H]ethylmaleimide, whereas that treated with ferricyanide was not. The ferricyanide-treated proOmpA was translocated into membrane vesicles in the presence of .DELTA.~.mu.H+. The mature OmpA thus translocated and processed was not labeled with N-[3H]ethylmaleimide. It is concluded that proOmpA possessing the Cys290-Cys302 disulfide bridge can be translocated without cleavage of the bridge, when .DELTA.~.mu.H+ is imposed. The accumulation of the disulfide bridge-contg. intermediate was ATP-dependent, whereas its conversion to the translocated mature form was not blocked in the presence of adenosine 5'-(.beta.,.gamma.-imino)triphosphate. Thus, the early and late stages of the translocation reaction require ATP and .DELTA.~.mu.H+ differently.m 0021-9258Translocation of proOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization&Journal of Biological Chemistrye 26528 17341-17347Tokyo 113, Japan 7738Tani, K. Mizushima, S. 1991D=ACHROMOBACTER-LYTICUS M497-1 OMPA PROTEINS PROTEOLYTIC-ENZYME A Chemically Cross-Linked Nonlinear proOmpA Molecule Can Be Translocated into Everted Membrane Vesicles of Escherichia-Coli in the Presence of the Proton Motive Force FEBS Letters 285S1127-131. 8 Jul- 7740PITanigawa, G. Orci, L. Amherdt, M. Ravazzola, M. Helms, J.B. Rothman, J.E.p 1993ADP-RIBOSYLATION FACTOR BINDING-PROTEIN BREFELDIN-A CHOLERA-TOXIN CLATHRIN COATOMER GUANINE-NUCLEOTIDE STACK SUCCESSIVE COMPARTMENTS VESICULAR TRANSPORTd^Hydrolysis of Bound GTP by ArF Protein Triggers Uncoating of Golgi-Derived COP-Coated VesiclesJournal of Cell Biologye 123m6 1365-1371 Decl 7741"Taniuchi, H. Anfinsen, C.B.h 1966The amino acid sequence of an extracellular nuclease of Staphylococcus aureus. I. Linear order of the fragments produced by cleavage with cyanogen bromide&Journal of Biological ChemistryN 24119 4366-4385y 10 Oct 7747,%Taniuchi, H. Anfinsen, C.B. Sodja, A. 1967xrNuclease-T: an active derivative of staphylococcal nuclease composed of two noncovalently bonded peptide fragments583 1235-1242 SeptVOProceedings of the National Academy of Sciences of the United States of Americad 7746,%Taniuchi, H. Anfinsen, C.B. Sodja, A. 1967The amino acid sequence of an extracellular nuclease of Staphylococcus aureus. II. The amino acid sequences of tryptic and chymotryptic peptides&Journal of Biological Chemistrye 242 20 4736-4751 25 Oct)1998*9*9+9)9*9+9+9+9+9+9+9,9,9*9,9,9+9*9, 9+9+@9+B9, 9,9*9)9+9+9,9+9*9)9,9,9,9+9+9,"9+9+9,&9+-9+,9,(9,)9,+9,,9,29+9,59+9+9+9+9+9+9+9+9+9+9+9+94A1>N2/$ 332081Hoyt, D.W. Cyr, D.M. Gierasch, L.M. Douglas, M.G.u 1991BLOCKS IMPORT ESCHERICHIA-COLI F1-ATPASE BETA-SUBUNIT INNER MEMBRANE PRECURSOR PROTEINS PROTEIN IMPORT SEQUENCES SIGNAL PEPTIDES TARGETING FUNCTION YEAST MITOCHONDRIAThe transport of the F1-ATPase beta-subunit precursor into mitochondria is dependent upon a presequence at its amino terminus. Within the mitochondrial membrane translocation site the potential amphiphilic character of the presequence region may be necessary to stabilize binding to the mitochondrial inner membrane. To better understand its role in protein import, the interaction of the F1-beta-presequence with lipid membranes was measured using circular dichroism and surface tensiometry. These studies reveal that a 20-residue peptide containing the F1-beta-presequence binds to phospholipid vesicles (K(d) = 4.5-6.0 x 10(-8) M) and adopts a predominantly alpha-helical structure. Although the presequence peptide binds avidly to lipids, it does not appear to penetrate deeply into the bilayer to perturb a reporter probe in the membrane interior. Compared with the effect of the peptides with demonstrated membrane insertion and lytic properties, the F1-beta-presequence appears to displace phospholipid head groups but not insert deeply into the bilayer. High concentrations (> 50-mu-M) of presequence peptides are required to noticibly perturb import of the full length F1-alpha- or F1-beta-subunit precursors. Thus, the F1-beta-presequence alone is not sufficient to efficiently compete for import but may require a protein context or a minimal length to assist insertion into the transport site. These observations are discussed in light of the different requirements for import of various presequence containing precursors into mitochondria.XRInteraction of Peptides Corresponding to Mitochondrial Presequences with Membranes&Journal of Biological Chemistry  266 32 21693-216993 15 Nov*#Hhfeld, J. Minami, Y. Hartl, F.-U. 1995TNHip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle Cell83589-598 jlfHhfeld, J. Jentsch, S. 1997VOGrpE-like regulation of the hsc70 chaperone by the anti-apoptotic protein BAG-1 Embo J1620 6209-62169321400XRhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=9321400'ZMBH, Zentrum fur Molekulare Biologie, Universitat Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany. j- hoehfeld@sun0.urz.uni-heidelberg.de*$Hhfeld, J. Cyr, D. M. Patterson, C. 2001hbFrom the cradle to the grave: molecular chaperones that may choose between folding and degradationEMBO Rep210885-890.11600451http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11600451 http://embo-reports.oupjournals.org/cgi/content/full/2/10/885 http://embo-reports.oupjournals.org/cgi/content/abstract/2/10/885'Institut fur Zellbiologie, Rheinische Friedrich-Wilhelms-Universitat Bonn, Ulrich-Haberland-Strasse 61a, D-53121 Bonn, Germany. hoehfeld@uni- bonn.de81Hribar, B. Southall, N. T. Vlachy, V. Dill, K. A.i 2002,&How ions affect the structure of water J Am Chem Soci 12441 12302-12311\ Oct 1612371874 JAHlehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12371874e'tnContribution from the Faculty of Chemistry and Chemical Technology, University of Ljubljana, Askerceva 5, 1000 Ljubljana, Slovenia, Graduate Group in Biophysics, University of California, San Francisco, California 94143-1204, and Department of Pharmaceutical Chemistry and Graduate Group in Biophysics, University of California, San Francisco, California 94143-1204. 3323 Hruby, V.J. 1993AMINO-ACIDS ASYMMETRIC-SYNTHESIS DEAMINO-OXYTOCIN DELTA-OPIOID RECEPTORS DYNAMIC CONSIDERATIONS OPTICALLY PURE ISOMERS RESTRICTED ANALOGS SELECTIVITY SOMATOSTATIN ANALOGS SPECIFICITYd]Conformational and Topographical Considerations in the Design of Biologically Active Peptides Biopolymers337@ 1073-10820 Juls in the molten globule appear to cause only individual helices to unfold, without significantly influencing the other helices or the overall topology. Thus, the key determinants of a protein's overall fold may not be of the all-or-none type. Nature Structural Biology SJET82Schulman, B.A. Kim, P.S. Dobson, C.M. Redfield, C. 1997XQA residue-specific NMR view of the non-cooperative unfolding of a molten globule. Nature Structural Biology48 630-634 SJEo1 JSa1a)Qa0ha0a'Na1$a[a a$a/-a1a1)a1a10a0aa a/}a0ala0a)Ma0a/aXa0a*;a17a1:a1;a1=a1?a1@a1Aa1Ba1Ca1Da1Ea1Fa1Ia1Ka1Ma1Na1Pa1Ra1Ta1Ua1Wa1Xa1Ya1[a1\a1]a1_a1`a1ca1da1ea1ga1ia1ia1ia INtermediates M M M M M M M5 MS M M M M+ M5 M< M M M; MG M_ M M  M r M { M | M* M#} M$c M$ M% M& M& M& M+ M+ M+ M) M* M+ M' M M( M( M* M M M#I M+E M& Md M) Mb M, M, M M, M& M, M, M, M, M _ ^ \ ] [ Z Yr X,.3"Figueroa, I.D. Russell, D.H. 1999~xMatrix-assisted laser desorption ionization hydrogen/deuterium exchange studies to probe peptide conformational changes.:4Journal of the American Society of Mass Spectrometry10719-731  SJEd 2221}Fijalkowska, I. Babinska, A. Ligocka, A. Plucienniczak, G. Plucienniczak, A. Stec, W. Okruszek, A. Wilk, A. Cierniewski, C.S. 1993ACTIVATION ANTIBODY BLOOD COAGULATION BOVINE PLASMA CONFORMATION FACTOR-V FUSION PROTEIN INACTIVATION MONOCLONAL-ANTIBODIES OLIGODEOXYRIBONUCLEOTIDES PROTEIN-C PROTEIN-C HEAVY CHAIN PURIFICATION THROMBIN nhAntibodies to Recombinant Fragment 212-276 of Protein-C Specifically Recognize the Intact Human Molecule$Biochimica et Biophysica Actao 1161 2-3n187-193P 13 Feb 2222&Fikes, J.D. Bassford, P.J., Jr.d 1989:3ESCHERICHIA GENE MALTOSE MUTATION PRLD PROTEIN SECA Mutations previously designated prlD were described that suppressed malE signal sequence mutations and were located in the vicinity of the secA gene on the Escherichia coli chromosome. It was shown that 4 such independently isolated prlD mutations represented 3 unique single-base substitutions in secA, resulting in alterations at residues 111, 373, and 488 of the 901-residue SecA protein. Heretofore, the only mutations that had been described for secA were located early in the gene and resulted in a general protein export defect. Insertion mutations in the cloned X-secA operon that reduced or eliminated suppression by a prlD mutation also were obtained. The properties of these suppressor and insertion mutations provide some insight into the role of SecA in the protein export process. 0021-9193nhNovel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide 1711p402-409 Chapel Hill, NC 27514, USAJournal of Bacteriology 2223TNFilhol, O. Baudier, J. Delphin, C. Louemackenbach, P. Chambaz, E.M. Cochet, C. 1992BETA-SUBUNIT CALF THYMUS CARCINOMA-CELLS CATALYTIC SUBUNIT EPIDERMAL GROWTH-FACTOR LARGE T ANTIGEN ONCOGENE SV40-TRANSFORMED CELLS TRANSFORMATION WILD-TYPECasein Kinase-II and the Tumor Suppressor Protein P53 Associate in a Molecular Complex That Is Negatively Regulated upon P53 Phosphorylation&Journal of Biological Chemistryn 267129 20577-20583 15 Oct 2228LEFilimonov, V.V. Privalov, P.L. Hinz, H.J. von der Haar, F. Cramer, F. 1976zsCALORIMETRY. DRUG STABILITY. HEAT. ISOLEUCINE. KINETICS. MAGNESIUM #RNA, TRANSFER. SACCHAROMYCES CEREVISIAE. SERINEM^WCalorimetric investigations on thermal stability of tRNAIle (yeast) and tRNASer (yeast)t& European Journal of Biochemistry701 25-31c 1 Novs 2226$Filimonov, V.V. Privalov, P.L. 1978LE#CALORIMETRY, DIFFERENTIAL SCANNING. POLY A. POLY A-U. THERMODYNAMICS<5Thermodynamics of base interaction in (A)n and (A.U)nS 122y4465-470 15 Jul"Journal of Molecular Biology 2224>7Filimonov, V.V. Pfeil, W. Tsalkova, T.N. Privalov, P.L. 1978ANIMAL. CALCIUM. CALORIMETRY. CARP. HYDROGEN-ION CONCENTRATION #MUSCLE PROTEINS. PARVALBUMINS. PROTEIN BINDING. PROTEIN CONFORMATION PROTEIN DENATURATION. TEMPERATURE. THERMODYNAMICSXQThermodynamic investigations of proteins. IV. Calcium binding protein parvalbuminBiophysical Chemistry82117-122 May 2227@:Filimonov, V.V. Privalov, P.L. Glangloff, J. Dirheimer, G. 1978#ACID DENATURATION. RNA, TRANSFER. SACCHAROMYCES CEREVISIAE ASPARTIC ACID. CALORIMETRY, DIFFERENTIAL SCANNING. MAGNESIUM. NUCLEIC [ANALYSIS]. THERMODYNAMICSLFA calorimetric investigation of melting of tRNAAsp from brewer's yeast$Biochimica et Biophysica Actar 521s1209-216a 21 Nov 2225B;Filimonov, V.V. Potekhin, S.A. Matveev, S.V. Privalov, P.L.l 1982#BIOPOLYMERS. CALORIMETRY, DIFFERENTIAL SCANNING. ENGLISH ABSTRACT #MACROMOLECULAR SYSTEMS. MATHEMATICS. MOLECULAR CONFORMATION THERMODYNAMICSyThermodynamic analysis of scanning microcalorimetry data. 1. Algorithms for deconvolution of heat absorption curves [Rus] Molekuliarnaia Biologiia163551-562May-Jun '0+,'.'/'-|/='+',v>=$<N.k<5Carey, J. Cameron, V. de Haseth, P.L. Uhlenbeck, O.C. 1983^XSequence-Specific Interaction of R17 Coat Protein with Its Ribonucleic Acid Binding Site Biochemistry22 2601-2610p 1000"Carlacci, L. Englander, S.W. 1993ALPHA-HELICES CONFORMATION ENERGETIC APPROACH EXCHANGE MODEL NUCLEAR MAGNETIC-RESONANCE OPTIMIZATION PACKING PREDICTION SPECTROSCOPYPIThe Loop Problem in Proteins - A Monte-Carlo Simulated Annealing ApproachE BiopolymersP338 1271-1286 AugN 1001LFCarlino, A. Toledo, H. Skaleris, D. Delisio, R. Weissbach, H. Brot, N. 1992ADP-RIBOSYLATION CALCIUM IONOPHORES CHAIN BINDING-PROTEIN CHICK-EMBRYO FIBROBLASTS GLUCOSE-REGULATED PROTEIN MAMMALIAN-CELLS PEPTIDE BINDING PURIFICATION STRESS PROTEIN STRESS PROTEINS TRANSPORTxqInteractions of Liver Grp78 and Escherichia-Coli Recombinant Grp78 with ATP - Multiple Species and Disaggregatione896t 2081-2085t 15 MarVOProceedings of the National Academy of Sciences of the United States of AmericaF@Carlone, R.L. Boulianne, R.P. Vijh, K.M. Karn, H. Fraser, G.A.D. 1993tmRetinoic Acid Stimulates the Synthesis of a Novel Heat Shock Protein in the Regenerating Forelimb of the Newt71 1-2 43-50Jan-Feb 1002AMPHIBIAN LIMB DIFFERENTIATION GEL-ELECTROPHORESIS GENE-EXPRESSION HEAT-SHOCK HOMEOBOX GENES HSP70 GENE IDENTIFICATION LIMB REGENERATION NEWT PATTERN FORMATION RECEPTOR RETINOIC ACID$Biochemistry and Cell BiologyR"Carlson, J.H. Silhavy, T.J.d 1993xqSignal Sequence Processing Is Required for the Assembly of LamB Trimers in the Outer Membrane of Escherichia-ColiJournal of Bacteriologyd 17511 3327-3334d JunP 1003|vCELLS EXPORT EXPRESSION GENE MALTOSE BINDING PROTEIN MUTATIONS OMPF PORIN PHAGE SHOCK PROTEIN PLASMA-MEMBRANE RECEPTOR Carlsson, U. Jonsson, B.H. 1995`Folding of b-sheet proteins.     5^482-487Q beta,%Current Opinion in Structural Biology SJErkCaroll, A.S. Gilbert, D.E. Liu, X. Chung, J.W. Michnowicz, J.E. Wagner, G. Elleberger, T.E. Blackwell, T.K.r 1997RLSKN-1 domain folding and basic region monomer stabilization upon DNA bindingGenes and Developmente11 2227-2238d 1006.(Carpenter, P.B. Hanlon, D.W. Ordal, G.W. 19924.5 S-RNA BASAL BODY COMPLEX CHEMOTAXIS ESCHERICHIA-COLI EXPRESSION FLAA LOCUS MUTANTS SALMONELLA-TYPHIMURIUM SEQUENCE SIGNAL RECOGNITION PARTICLEZTflhF, a Bacillus-Subtilis Flagellar Gene That Encodes a Putative GTP-Binding ProteinMolecular Microbiology618 2705-2713t Sep 1004haCarpenter, C.L. Auger, K.R. Chanudhuri, M. Yoakim, M. Schaffhausen, B. Shoelson, S. Cantley, L.C.o 1993FACTOR-I RECEPTOR MIDDLE-T ANTIGEN PDGF RECEPTOR PHOSPHATIDYLINOSITOL KINASE-ACTIVITY PHOSPHORYLATION POLYOMAVIRUS PROTEIN RECEPTOR TYROSINE KINASES SIGNAL TRANSDUCTION TRANSFORMATION`rlPhosphoinositide 3-Kinase Is Activated by Phosphopeptides That Bind to the SH2 Domains of the 85-kDa Subunit&Journal of Biological Chemistry 268r13 9478-9483 5 May 1005ZTCarpenter, C.L. Auger, K.R. Duckworth, B.C. Hou, W.M. Schaffhausen, B. Cantley, L.C. 1993BETA-RECEPTOR CELLS I PHOSPHATIDYLINOSITOL KINASE MIDDLE-T ANTIGEN PHOSPHORYLATION PP60C-SRC PURIFICATION RECEPTOR TYROSINE KINASES SIGNAL TRANSDUCTION TRANSFORMATIONhaA Tightly Associated Serine/Threonine Protein Kinase Regulates Phosphoinositide 3-Kinase Activityp$Molecular and Cellular Biology133` 1657-1665P MarJCCarpenter, K.A. Wilkes, B.C. Lean, A.D. Fournier, A. Schiller, P.W. 1997Hydrophobic forces are responsible for the folding of a highly potent natriuretic peptide analogue at a membrance mimetic surface: an NMR study Biopolymers42 37-48/ JAH $Carpenter, C.L. Cantley, L.C.d 1998&A flattened face for membranes. Nature Structural Biologyd5r843-845  SJEd 1007PJCarpentier, J.L. Paccaud, J.P. Baecker, J. Gilbert, A. Orci, L. Kahn, C.R. 1993COATED PITS CULTURED HUMAN-LYMPHOCYTES CYTOPLASMIC DOMAIN FACTOR-II RECEPTOR GROWTH-FACTOR LOW-DENSITY LIPOPROTEIN PLASMA-MEMBRANE RAPID INTERNALIZATION SURFACE REDISTRIBUTION TYROSINE KINASE-ACTIVITYd]Two Steps of Insulin Receptor Internalization Depend on Different Domains of the beta-Subunit5Journal of Cell Biology 122i6 1243-1252 Sepl-T Molecular-V E-W E-X E-Y E-Z E-k E-m E E- E+ E  E , E E  E} E- E- E- E- E- E- E, E, E-O E- E- E- E- E- E- E- E- E- E- E- E- E- E- E- E.$ E.1 E.6 E.< E.? E.C E E E.E E.M E.S E.[ E.\ E.] E./ E.e E.f E.m E.w E. E. E. E. Eamontano, A. Chothia, C. Lesk, A.M. 1990z3-DIMENSIONAL STRUCTURE ANTIBODY-ANTIGEN COMPLEX COMPLEMENTARITY CRYSTAL-STRUCTURE FRAGMENT PROTEINS REFINEMENT RESOLUTIONFramework Residue-71 Is a Major Determinant of the Position and Conformation of the 2nd Hypervariable Region in the Vh Domains of Immunoglobulins 2151175-182 5 Sep"Journal of Molecular Biology 7928 Tramontano, A. Lesk, A.M.0 19923-DIMENSIONAL STRUCTURE COMPLEX CRYSTAL-STRUC200v00 0)070>0m0t00Q0h0000b0x0000000 "0 20 L0 f0 j0 w0 }0 0 0 0 0!0!0!0!0"0")0"G0"0"0#k0#j0#0#0#0$O0$`0$c0$0$0%0%)0%f0%0%0&0&0&0&0&0&0 ! 爈" ﮮ( ! ?  !/"(  ﯺ **꯿￫    %  $/HTtp0/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u/u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u0u $嵷뻿% !寷*뿿 﫭寯 "*"" !뺫 $ % %("> ! !ﻧ % " $ 孷"%*﷿ $ 祥 !fR a a;a ~a#a$a5a=aa a a aG a-z a/I a2 aaaawaa +a aaaaaaa a$!aaaaa01 1 1 1 1)1 14112111I1B11 11$1111!D1#/1#1)(1)-1))1+_1+1+1+1@withg YYY"Y$Y%Y2Y3YCYVY^YdYY(YYYYYYYYYYYYYY)Y1Y;YLYOYcYyYY*YYYYYYYVdiOxide pHENYLHEXATRIENE'theriaGolerecteTedsBss,s l!olyascMrIMINAteeases s ss-cp es)smutaseppersionseruptedesociate! ionLvedn TAncei+6s6incto Xo5ortingr-ributionS  SMulfideo  s& s s phidethiophosphatesIvErsIons&?'ision :m28NAKKK K $KKmKK'K JQJ_Kserver... Connecting to host... Client message sent The Host closed the connection. Retrieving references 31 - 33... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving reference number 34... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Done retrieving references Done Connecting to host... Connecting to hA CAAX or a CAAL Motif and a Second Signal Are Sufficient for Plasma Membrane Targeting of ras ProteinsD EMBO Journal1013 4033-4039 Deci 2963<6Handel, T.M. Williams, S.A. Menyhard, D. Degrado, W.F. 1993f_DENOVO DESIGN INTERMEDIATE MOLTEN-GLOBULE STATE POLYPEPTIDE PROTEIN DESIGN STABILITY TRYPTOPHANHAIntroduction of a Trp Residue into alpha-4 as a Probe of DynamicsL.(Journal of the American Chemical Society 115L11 4457-4460 2 Jun  1665HADenesyuk, A.I. Vihinen, M. Lundell, J. Zavyalov, V.P. Korpela, T.o 1993xqESCHERICHIA-COLI FKBP IMMUNOSUPPRESSANT FK506 INHIBITION NMR PEPTIDYL-PROLYL ISOMERASE PROTEIN RAPAMYCIN RECEPTORf`Structural Similarity of the Binding Sites of Cyclophilin A-Cyclosporin-A and FKBP-FK506 Systems:3Biochemical and Biophysical Research Communicationsn 192o2912-917 30 Apr 1666f`Deneve, M. Deloose, M. Jacobs, A. Vanhoudt, H. Kaluza, B. Weidle, U. Vanmontagu, M. Depicker, A. 1993ARABIDOPSIS-THALIANA CAMV 35S PROMOTER CELLS CHAIN CREATINE-KINASE EXPRESSION FAB FRAGMENT GEL GENES HEAVY INTER-TRANSFORMANT VARIABILITY MONOCLONAL-ANTIBODY NICOTIANA-TABACUM PROTEINS SELF-ASSEMBLY TRANSGENIC PLANTS\VAssembly of an Antibody and Its Derived Antibody Fragment in Nicotiana and ArabidopsisTransgenic Research24227-237 Jul 166982Denfert, C. Wuestehube, L.J. Lila, T. Schekman, R. 1991ADP-RIBOSYLATION FACTOR COMPLEX ENDOPLASMIC-RETICULUM GENE GOLGI-APPARATUS POLYACRYLAMIDE GELS SECRETORY VESICLES VESICULAR TRANSPORT YEAST YPT1 YPT1 PROTEINH}Sec12p-Dependent Membrane Binding of the Small GTP-Binding Protein Sar1p Promotes Formation of Transport Vesicles from the ER Journal of Cell Biology  1144E663-670a Aug` 1667D=Denfert, C. Barlowe, C. Nishikawa, S. Nakano, A. Schekman, R.  1991DETERMINANTS DNA GENES GOLGI-APPARATUS GTP-BINDING PROTEIN MACHINERY SACCHAROMYCES-CEREVISIAE SEQUENCES TRANSPORT YEAST SECRETORY PATHWAYiSec12p is a membrane glycoprotein required for the formation of a vesicular intermediate in protein transport from the endoplasmic reticulum to the Golgi apparatus in Saccharomyces cerevisiae. Comparison of the N-linked glycosylation of Sec12p, a Sec12p-invertase hybrid protein, and a derivative of Sec12p lacking 71 carboxy-terminal amino acids showed that Sec12p is a type II membrane protein. Analysis of two truncated forms of Sec12p and of a temperature-sensitive mutant indicated that the C-terminal domain of Sec12p is not essential for protein transport, whereas the integrity and membrane attachment of the cytoplasmic N-terminal domain are essential. Expression of a soluble cytoplasmic domain dramatically inhibited the growth of a sec12 temperature-sensitive strain by increasing the transport defect at a normally permissive temperature. This growth inhibition as well as the sec12 temperature-sensitive defect were suppressed by the overproduction of Sar1p, a small GTP-binding protein that participates in protein transport. Sar1p membrane association was enhanced by elevated levels of Sec12p. These results suggest that the cytoplasmic domain of Sec12p interacts with Sar1p and that the complex may function to promote vesicle formation.{Structural and Functional Dissection of a Membrane Glycoprotein Required for Vesicle Budding from the Endoplasmic Reticulum$Molecular and Cellular Biology1111 5727-57341 Nov 1668,%Denfert, C. Gensse, M. Gaillardin, C. 1992ARABIDOPSIS-THALIANA ENDOPLASMIC-RETICULUM FUSION PROTEIN GTP-BINDING PROTEIN MEMBRANE GLYCOPROTEIN MOLECULAR-CLONING SACCHAROMYCES-CEREVISIAE SCHIZOSACCHAROMYCES-POMBE SECRETION SECRETORY PATHWAY SEQUENCE-ANALYSIS TRANSPORT VESICLES VESICULAR TRANSPORTiFission Yeast and a Plant Have Functional Homologues of the Sar1-Protein and Sec12-Protein Involved in ER to Golgi Traffic in Budding Yeastn EMBO Journal1111 4205-4211 Novi 1670Deng, T.L. Karin, M. 1992AFFINITIES COMPLEXES DIMERIZATION DNA-BINDING DNA-BINDING PROTEIN FAMILY FOS LEUCINE-ZIPPER PHOSPHORYLATION RECOGNITION REPRESSOR TRANSACTIVATION~xConstruction and Expression of a Monomeric-c-Jun Protein That Binds and Activates Transcription of AP-1-Responsive Genes8918 8572-8576a 15 SepVOProceedings of the National Academy of Sciences of the United States of Americat OXygenaser t t t! t! t"K t" t# t tE t#0 t# t84 ttedion" H  s sHP haemoglobinOEE% EMOGLOBINSllhl l l cllEllz luciferin5tocan intPuPPPPPbPeP RRRRRR,RRICHA#yaggimCmat.ler7^s#sterz#zDzakit.Urowski~Yto!~wa0whan3kan,olsPA(Aaa 2$2%2)2*2+2+2Ellz luciferin5tocan intPuPPPPPbPeP RRRRR,RRRICHAyagiCmatDzakiYtoPA(Aaa 2$2%2)2*2+22450x1&1 1 #1111e111 111&1!51%1+1,1161L1-11 1%1k111~11O1b1!41!31#b1%1%161 j11700j0k1l23m4%4nIo56p7 7q8r889tCC%AME~IIE1%S10 0`0x0#000A0000"0$0"0-0209 0909)00E01%1k111~11O1b1 j110j0k1l23m4%4nIo56p7 7q8r8t9C~IIE1110 0`0x0#000A00000E000 h Recognition/7 g,b g+t g/ g/ g0> g0 g0 g1 g1  g/9 g)0 g)/ g/ g" g1 g g1 g g* g g& g@ g= g2 g0 g0h g'N g0g g0 g  g/} g0 g0 g1, g1 g2 g2 g2 g2 g2 g2 g2 g2 g2 g3  g3 g3& g3Z g3 g4 g4 g4 g45 g4L g5 g5 g5 g5 g6 g6 g6 g6 g7] g7a g7m g7r g7{ g7| g7~ g7 g7 g7 g7 g7 g7 g8* g85 g8H g8X g8Z g8{ g8| g8 g9` g"r g.$ g0^ g g gN' gg0 g0 g  g}/ g0 g0 g,1 g1 g2 g2 g2 g2 g2 g2 g2 g2 g2 g 3 g3 g&3 gZ3 g3 g4 g4 g4 g54 gL4 g5 g5 gr" g$. g^0 g g gg$Y$$*}X$(Y$2$M $k$}'$|)$+$|$}*%/%`%]%d~'(%~%%%%%%%%%%%%%%%%%4%3%G%l%%%%%8&;&H&CL&B&=&M&O &N &d&>&T&h&g&&x&w&sX&yY&|]7Schusterstkowski*0 t/ t/ t2 tturkensnman wwab0emenacherel'Hlbe(n'_n-l2ll4l6Wlolerndergingerrtziiiz z z z jz z zb(bDbb*bb)bpbbbbOb-b/ob8b8Zbbachmmanz i eBeeeeqesere e e4Ringer1 e*edinger5fhme%Oigeriger* resolution N N( NM N N N N Nu N N N< N N N N N*" N  N  N  N C N V N W N X N  N7 NW N N N NJ N N N N  N*R N N) N N N N N N# N N N N N N NP NO N N*# N N*P N N[ N N N. N. NdK IsOmeraseSh+ i+ i#L i/ i/ i/ i)/ i4o i6 i71 i#L iics6(s {sationm$ mm Z z. zE z z z  z  z  zD z z2 z zc z z! z{ z z  z4o z6  z6G z8B z8 z8 zGzations s s s  s  s N s] s* su s s s so s* s s s s s+A s s] s s& s*s s  s+ s, s*0 s s/ s.?1<3]rez/query?db=m&form=6&dopt=r&uid=11801005$Adcox, K. Adler, S. S. Ajitanand, N. N. Akiba, Y. Alexander, J. Aphecetche, L. Arai, Y. Aronson, S. H. Averbeck, R. AwesB7Stereochemical quality of protein structure coordinates0*Proteins: Structure, Function and Genetics124 345-364 Apr` 5311CHI-1 ANGLES CONFORMATION CRYSTAL-STRUCTURE CRYSTALLOGRAPHY ERRORS FEATURES GLOBULAR-PROTEINS MODEL PHI,PSI-DISTRIBUTION PROTEIN-STRUCTURE REFINEMENT RESOLUTION STRUCTURE SECONDARY STRUCTURE STEREOCHEMICAL PARAMETERS 5315 Morris, K.F. Johnson, C.S. 1992ELECTROPHORETIC NMRtLFMobility-Ordered 2-Dimensional Nuclear Magnetic Resonance Spectroscopy.(Journal of the American Chemical Society 1142e776-777r 15 Jan 5316HAMorris, S.A. Schroder, S. Plessmann, U. Weber, K. Ungewickell, E.t 1993AP180 ASSEMBLY PROTEINS AUXILIN BOVINE BRAIN CLATHRIN-COATED VESICLES COATED VESICLES COMPONENT KINASE MOUSE PHOSPHOPROTEIN F1-20 NP185 PHOSPHORYLATION PLASMA-MEMBRANE PURIFICATION2+Binding of AP180 to clathrin triskelia induces their assembly into 60-70 nm coats. The largest rat brain cDNA clone isolated predicts a molecular weight of 91 430 for AP180. Two cDNA clones have an additional small 57 bp insert. The deduced molecular weight agrees with gel filtration results provided the more chaotropic denaturant 6 M guanidinium thiocyanate is substituted for the weaker guanidinium chloride. The sequence and the proteolytic cleavage pattern suggest a three domain structure. The N-terminal 300 residues (pI 8.7) harbour a clathrin binding site. An acidic middle domain (pI 3.6, 450 residues), interrupted by an uncharged alanine rich segment of 59 residues, appears to be responsible for the anomalous physical properties of AP180. The C-terminal domain (166 residues) has a pI of 10.4. AP180 mRNA is restricted to neuronal sources. AP180 shows no significant homology to known clathrin binding proteins, but is nearly identical to a mouse phosphoprotein (F1-20). This protein, localized to synaptic termini, has so far been of unknown function.|vClathrin Assembly Protein-AP180 - Primary Structure, Domain Organization and Identification of a Clathrin Binding Site EMBO Journal122667-675 Feb,%Morris, J. R. Keep, N. H. Solomon, E.  2002RKIdentification of residues required for the interaction of BARD1 with BRCA1/ J Biol Chemc 277l119382-6.11773071 JAHhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11773071 http://www.jbc.org/cgi/content/full/277/11/9382 http://www.jbc.org/cgi/content/abstract/277/11/93827 5317.'Morrison, R.P. Su, H. Lyng, K. Yuan, Y. 1990B7Morshauser, R.C. Wang, H. Flynn, G.C. Zuiderweg, E.R.P.X 1995leThe Peptide-Binding Domain of the Chaperone Protein Hsc70 has an Unusual Secondary Structure Topology Biochemistry34 6261-6266 5318NGMorshauser, R.C. Hu, W. Wang, H. Pang, Y. Flynn, G.C. Zuiderweg, E.R.P. 1999zsHigh-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70."Journal of Molecular Biology 289 1387-1403X SJE$] Structure$ s*E s% s% s% s) s& s& s& s&r s& s+ s+ s sO sN s, s,6 s) s*s s  s,K s,P s,Q s,R s,[ sl s- s- s s U sU s s$ sA s-q s s- s- s- s- s- s. s. s. s. s.P s. s. s s- s- sE s s( s/ s/ s/ si s0 s0 s0 s/Jbc0C0C0C0C0C0C0C0C0C0C1C1C0C+ C0C0C1EC1OC1RC1bC1cC1dC1eC1gC1pC1rC1{C1C1C1C1C2C2C2C2C2C2]C2sC2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C2C3C3C3'Biology4'u4'u42'u48'u45'u4C'u4?'u4N'u4R'u4S'u4V'u4g'u4n'u4p'u4u'u4'u4'u4'u4'u4'u4'u4'u4'u4'u4s'u4'u4'u4'u4'u4'u1'u5E'u5G'u5I'u5H'u5P'u5O'u5Y'u5\'u5b'u5a'u5k'u5i'u5p'u5'u5'u5'u5'u5'u1'u5'u5'u5'u5'u5'u5'u5'u5'u5'u5'u5'u5'u5article5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d5d6d6d6d6d6d6d6d6d6 d6 d6 d6 d6d6d6d6d6d6d6d6d6d6d6d6d6d6 d6!d6"d6#d6%d6&d6'd6(d6)d6)d6)d"n Tronrud1986 Tronrud1987"p Tronrud1987 Tronrud1989$9 Tronrud1990 Tronrud1992 z Tropschug1990"q Tropschug1990& Tropschug1991$ Tropschug1991L Tropschug1991 Tropsha1991"r Tropsha1992% Tropsha1993, Tropsha1998 Trotman1992' Trouard1990/a Troullier2000/ Troullier2000 Troung19939 Troutt1991 Troutt1992  Troutt1992  Trowbridge1990  Trowbridge1991 "s Trowbridge1991 "t Trowbridge1993  Trowsdale1991 Trowsdale1991o Trowsdale1992 Troxell1992 Truckses1992 Truckses1996#qTruckses19966TTrudelle19929!Trudelle19934Trudelle19933 Truhlar2002.Trujillo1997 zTrulzsch199005Trulzsch19919 Trumble1993Trumppkallmeyer1993"u Trun1987"v Trun1988v"x Trun1989"w Trun1989v Trun19929! Trunk1992"y Truong1991  Truong19922! Truong1993 !t Truong1993 Truong19939+ Truong19988P Trus19939\Truscott1992^Truscott1993]Truscott1993Truscott19938Truscott2002f Tsai1976v7 Tsai1991. Tsai19929K Tsai19929A Tsai19929A Tsai19929 Tsai19921 Tsai19939"z Tsai1993v? Tsai19933< Tsai19939"{ Tsai1996v8 Tsai19970* Tsai1998v. Tsai19989., Tsai1999 .e Tsai1999. Tsai199992 Tsai199992 Tsai2000,0o Tsai2001w3 Tsai20013 Tsai200113= Tsai200223Q Tsai200204 Tsai20025p Tsai200335y Tsai200308b Tsai2003a \Tsalkova197880Tsalkova1979"|Tsalkova1980"~Tsalkova1983"}Tsalkova1983"Tsalkova1985Tsalkova1991"Tsalkova1993-7Tsalkova1999x" Tsang1990%T Tsang1990" Tsang1991" Tsang1992 Tsang1993 Tsang1993 Tsang1993" Tsang1993+~ Tsang1994" Tsao1987v" Tsao1993v- Tsaprailis1999X Y Tsarbopoulos1992"Tschantz1993" Tschauder1992* Tschudin1989STschudin1990Tschudin1990#Tschudin19939" Tse1993% Tseng1994G Tsernoglou1976 J Tsernoglou1981  Tsernoglou1991 Tsfasman19919. Tsiang19967 Tsien19987 Tsien20007H Tsien20027 Tsien2002#fTsigelny1993,Tsigelny199888,Tsigelny2003n"Tsikaris1992"Tsikaris1993"Tsikaris1993" Tsilikounas1992" Tsirka1993 " Tsong1971" Tsong1972" Tsong1972" Tsong1972" Tsong1972M Tsong1990 Tsong19913 Tsong19923 Tsong1992, Tsong1996^ Tsou1991$ Tsou1993v% Tsou19933&N Tsou19933& Tsou19933/ Tsou1993v2 Tsu1993" Tsubaki1993" Tsubaki1993 Tsuda1991" Tsuda1992 Tsuda1993" Tsuge1991+ Tsuge1993" Tsugeki1992" Tsugeki1993 8 Tsui19838-R Tsui1999" Tsuji1987' Tsuji1991" Tsuji1993" Tsuji1993 Tsukamoto1991 Tsukamoto1992& Tsukamoto1992% Tsukita1993" Tsukiyama1994 Tsukuda19922C Tsumoto2001 Tsunasawa1992 Tsunasawa1993" Tsuneyoshi1991 " Tsuprun1991A Tsuprun1992" Tsuprun1992" Tsuprun1992" Tsuprun1992) Tsurupa1998- Tsurupo1997' Tsuruta1993( Tsuruta1995/ Tsuruta19950V Tsutsui1998dTsutsumi19939Tsutsumi19955 Tsygankov1992 Tuboi1990 Tuboi1991!U Tuboi1993 Tuboi1993n Tuchscherer1992" Tuchscherer1992" Tuchscherer1993 Tuchsen1992" Tuck1993v Tucker19911I Tucker1992 " Tucker1992 J Tucker1993 7Tucker-Kellogg2002FTuckwell19920WTuderman19833" Tuffery1991" Tuffery1993 Tufillaro19924- Tugarinov20025 Tugarinov20038= Tugarinov20038 Tugarinov20038 Tugarinov2003 Tuite1991 Tuite1993 Tuite1994) Tukalo19949 Tulip1989 Tulloch1990 Tuls19909 Tuls19919" Tuma1993v" Tuma1993vTumanyan19911" Tummino1993lTunemoto1992" Tung1990v| Tung19933" Tunon1992" Tuohy1990 Tuparev1992 Tuppy1952 Turck1991 Turck1992' Turck1992z Turck1993" Turck1993- Turecek1999 Turk1992/ Turk200002 Turley2002<2 Turley2002<*Turmaine19979 Turnbull1992  Turnell1990" Turnell1992" Turner1990 Turner19901~ Turner19911 Turner19919k Turner19929k Turner19929k Turner19929P Trus19939\Truscott1992^Truscott1993]Truscott1993Truscott1993 Tsai1976v. Tsai19929K Tsai19929A Tsai19929A Tsai19929 Tsai19921 Tsai19939"z Tsai1993v? Tsai19933< Tsai19939"{ Tsai1996v* Tsai1998v \Tsalkova197880Tsalkova1979"|Tsalkova1980"~Tsalkova1983"}Tsalkova1983"Tsalkova1985Tsalkova1991"Tsalkova1993" Tsang1990%T Tsang1990" Tsang1991" Tsang1992 Tsang1993 Tsang1993 Tsang1993" Tsang1993+~ Tsang1994" Tsao1987v" Tsao1993v Y Tsarbopoulos1992"Tschantz1993" Tschauder1992* Tschudin1989STschudin1990Tschudin1990#Tschudin19939" Tse1993% Tseng1994G Tsernoglou1976 J Tsernoglou1981  Tsernoglou1991 Tsfasman19919#fTsigelny1993"Tsikaris1992"Tsikaris1993"Tsikaris1993" Tsilikounas1992" Tsirka1993 " Tsong1971" Tsong1972" Tsong1972" Tsong1972" Tsong1972M Tsong1990 Tsong1991 Tsong1991^ Tsou1991$ Tsou1993v% Tsou19933&N Tsou19933& Tsou19933/ Tsou1993v2 Tsu1993" Tsubaki1993" Tsubaki1993 Tsuda1991" Tsuda1992 Tsuda1993" Tsuge1991+ Tsuge1993" Tsugeki1992" Tsugeki1993 8 Tsui19838" Tsuji1987' Tsuji1991" Tsuji1993" Tsuji1993 Tsukamoto1991 Tsukamoto1992& Tsukamoto1992% Tsukita1993" Tsukiyama1994 Tsukuda1992 Tsunasawa1992 Tsunasawa1993" Tsuneyoshi1991 " Tsuprun1991A Tsuprun1992" Tsuprun1992" Tsuprun1992" Tsuprun1992) Tsurupa1998' Tsuruta1993( Tsuruta1995dTsutsumi19939Tsutsumi19955 Tsygankov1992 Tuboi1990 Tuboi1991!U Tuboi1993 Tuboi1993n Tuchscherer1992" Tuchscherer1992" Tuchscherer1993 Tuchsen1992" Tuck1993v Tucker19911I Tucker1992 " Tucker1992 J Tucker1993 FTuckwell1992" Tuffery1991" Tuffery1993 Tufillaro1992 Tuite1991 Tuite1993 Tuite1994) Tukalo19949 Tulip1989 Tulloch1990 Tuls19909 Tuls19919" Tuma1993v" Tuma1993vTumanyan19911" Tummino1993lTunemoto1992" Tung1990v| Tung19933" Tunon1992" Tuohy1990 Tuparev1992 Tuppy1952 Turck1991 Turck1992' Turck1992z Turck1993" Turck1993 Turk1992*Turmaine19979 Turnbull1992  Turnell1990" Turnell1992" Turner1990 Turner19901~ Turner19911 Turner19919k Turner19929<:;h8F9Z6 7 1974(!Ellis, J. Murray, I.A. Shaw, W.V.s 1991ACTIVE-SITE MECHANISM~xReplacement by tyrosine or phenylalanine was used to assign the additive contributions of each of the three tryptophan residues of chloramphenicol acetyltransferase (CAT) to its intrinsic fluorescence on excitation at 295 nm. During the assessment of the fluorescence responses of the wild-type enzyme to the binding of ligands, it was found that the overlapping absorption spectra of chloramphenicol and tryptophan, with an attendant inner filter effect, required the use of a displacement technique involving an alternative substrate (the p-cyano analogue of chloramphenicol) without significant absorption at 295 nm. By the use of two-Trp, one-Trp, and Trp-less variants, in combination with this displacement technique, it was possible to demonstrate that Trp-86 and Trp-152 are involved in the fluorescence quenching associated with the binding of chloramphenicol, most likely via nonradiative energy transfer from these residues to the bound substrate. Trp-152 is mainly responsible for the fluorescence enhancement accompanying the binding of acetyl-CoA (and CoA) through proximity effects and solvent exclusion on substrate association.Intrinsic Fluorescence of Chloramphenicol Acetyltransferase - Responses to Ligand Binding and Assignment of the Contributions of Tryptophan Residues by Site-Directed Mutagenesis Biochemistry3044 10799-10805 5 Nov 1973("Ellis, J. Bagshaw, C.R. Shaw, W.V. 1991:4ACTIVE-SITE DIHYDROFOLATE-REDUCTASE ENZYME MECHANISMChloramphenicol acetyltransferase (CAT) catalyzes the acetyl-CoA-dependent acetylation of chloramphenicol by a ternary complex mechanism with a rapid equilibrium and essentially random order of addition of substrates. Such a kinetic mechanism for a two-substrate reaction provides an opportunity to compare the affinity of enzyme for each substrate in the binary complexes (1/K(d)) with corresponding values (1/K(m)) for affinities in the ternary complex where any effect of the other substrate should be manifest. The pursuit of such information for CAT involved the use of four independent methods to determine the dissociation constant (K(d)) for chloramphenicol in the binary complex, techniques which included stopped-flow measurements of on and off rates, and a novel fluorometric titration method. The binary complex dissociation constant (K(d)) for acetyl-CoA was measured by fluorescence enhancement and steady-state kinetic analysis. The ternary complex dissociation constant (K(m)) for each substrate (in the presence of the other) was determined by kinetic and fluorometric methods, using CoA or ethyl-CoA to form nonproductive ternary complexes. The results demonstrate an unequivocal decrease in affinity of CAT for each of its substrates on progression from the binary to the ternary complex, a phenomenon most economically described as negative cooperativity. The binary complex dissociation constants (K(d)) for chloramphenicol and acetyl-CoA are 4-mu-M and 30-mu-M whereas the corresponding dissociation constants in the ternary complex (K(m)) are 12-mu-M and 90-mu-M, respectively. Reasoning from the known binary complex structures, the 3-fold decrease in affinity of CAT for each of its substrates en route to the tetrahedral intermediate and the transition state may be a necessary prerequisite for their formation, probably involving subtle but important changes in the structure of the enzyme and/or the conformations of bound substrates.Substrate Binding to Chloramphenicol Acetyltransferase - Evidence for Negative Cooperativity from Equilibrium and Kinetic Constants for Binary and Ternary Complexes Biochemistry3044 10806-10813 5 Nov"Ellis, R.J. Vandervies, S.M. 1991Molecular Chaperones$Annual Review of Biochemistry60321-347  1983INCOMPLETE ATP HYDROLYSIS ESCHERICHIA-COLI GLUCOCORTICOID RECEPTOR HEAT-SHOCK PROTEIN MITOCHONDRIAL PROTEIN PRECURSOR PROTEINS RIBULOSE BISPHOSPHATE CARBOXYLASE STRESS PROTEINS SUBUNIT BINDING-PROTEIN 1979 Ellis, R.J. 1991ATP HYDROLYSIS BIOGENESIS GROEL HEAT-SHOCK MEMBRANE MITOCHONDRIA MOLECULAR CHAPERONES PRECURSOR PROTEINS RIBULOSE BISPHOSPHATE CARBOXYLASE TRANSLOCATIONHAChaperone Function - Cracking the Second Half of the Genetic CodeS Plant JournalP1r1 9-13 Jul Ellis, R.J. 1992&Cytosolic chaperonin confirmed. Nature 358191-192  1972 Ellis, J. 1992MOLECULAR CHAPERONES60Protein Folding - Cytosolic Chaperonin Confirmed Nature 358 6383191-192B 16 Jul 1971Ellis, E.M. Reid, G.A. 1993A-PROTEIN DOMAIN IMPORT RECEPTOR MITOCHONDRIAL BIOGENESIS NOP3 NPL3 NUCLEAR NUCLEOLAR PROTEIN OUTER-MEMBRANE PROTEIN PRECURSOR RECOGNITION RIBONUCLEOPROTEIN SUPPRESSOR VIABILITY YEAST YEAST MITOCHONDRIAyThe Saccharomyces Cerevisiae Mts1 Gene Encodes a Putative RNA-Binding Protein Involved in Mitochondrial Protein Targeting Gene 132c2175-183 15 Oct)C)    /  r f   3261Holm, L. Sander, C. 1992"2.0-A RESOLUTION BINDING CRYSTAL-STRUCTURE CRYSTALLOGRAPHIC REFINEMENT ESCHERICHIA-COLI EXCLUDED VOLUME APPROXIMATION FERREDOXIN GLOBULAR-PROTEINS HYDROPHOBIC EFFECT MODEL BUILDING MOLECULAR-STRUCTURE MONTE-CARLO OPTIMIZATION PANCREATIC PHOSPHOLIPASE-A2 SOLVENT CONTACT MODEL SURFACEAB;Evaluation of Protein Models by Atomic Solvation Preferencee 225e1 93-105 5 Maye"Journal of Molecular Biology 3260>7Holm, L. Ouzounis, C. Sander, C. Tuparev, G. Vriend, G. 1992JCA Database of Protein Structure Families with Common Folding MotifscProtein Sciencea112 1691-1698  DecP 32630)Holmes, M.A. Tronrud, D.E. Matthews, B.W.p 1983lfStructural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitor Biochemistry221236-240P 4 Janp Holmgren, A. 1984JCEnzymatic reduction-oxidation of protein disulphides by thioredoxin 107295-300Methods in Enzymology  3264<5Holmgren, A. Kuehn, M.J. Branden, C.I. Hultgren, S.J. 1992ADHESIN BIOGENESIS OF PILI CRYSTAL-STRUCTURE DOMAINS FRAGMENT GENE HUMAN CD4 IMMUNOGLOBULIN FOLD PATHOGENESIS PERIPLASMIC CHAPERONE PROTEIN RECEPTOR-BINDING RECOGNITION UROPATHOGENIC ESCHERICHIA-COLIpd^Conserved Immunoglobulin-Like Features in a Family of Periplasmic Pilus Chaperones in Bacteria EMBO Journal114a 1617-1622a Apr7 3265 Holtzer, M.E. Holtzer, A. 1990`YBETA BETA TROPOMYOSIN CIRCULAR-DICHROISM CLEAVAGE LEUCINE-ZIPPER MODEL PROTEINS STABILITYalpha-Helix to Random Coil Transitions of 2-Chain Coiled Coils - Experiments on the Thermal Denaturation of Isolated Segments of alphaalpha-Tropomyosin Biopolymers30 9-10985-993 3267 Holtzer, M.E. Holtzer, A. 1992AMINO-ACIDS CIRCULAR-DICHROISM HELICITY IONIC-STRENGTH PROTEIN SEGMENTS STABILITY STABILIZATION THERMAL-DENATURATION TROPOMYOSINzsalpha-Helix to Random Coil Transitions -Determination of Peptide Concentration from the CD at the Isodichroic Pointe Biopolymers3212 1675-1677 Dec 3266 Holtzer, M.E. Holtzer, A.p 1992AMINO-ACIDS CIRCULAR-DICHROISM IONIC-STRENGTH L-GLUTAMIC ACID OPTICAL ROTATORY DISPERSION PEPTIDE STABILITY STABILIZATION THERMAL-DENATURATION TROPOMYOSINvoalpha-Helix to Random Coil Transitions -Interpretation of the CD in the Region of Linear Temperature Dependencei Biopolymersi3211 1589-1591 NovPJHoltzer, M. E. Braswell, E. Angeletti, R. H. Mints, L. Zhu, D. Holtzer, A. 2000~Ultracentrifuge and circular dichroism studies of folding equilibria in a retro GCN4-like leucine zipper [In Process Citation]Biophysical Journal784 2037-2048lehttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.biophysj.org/cgi/content/full/78/4/203720200181 SJEe 3268"Holtzman, D.M. Mobley, W.C.B 1991RLAMYLOID PROTEIN-PRECURSOR BRAIN EXPRESSION NERVE GROWTH-FACTOR SECRETED FORM.(Molecular Studies in Alzheimer's Disease$Trends in Biochemical Sciences164140-144t Aprp 32690)Holwerda, B.C. Padgett, H.S. Rogers, J.C. 1992AMINO-ACIDS BARLEY ALEURONE LAYERS ENDOPLASMIC-RETICULUM GIBBERELLIC-ACID LYSOSOMAL-ENZYMES PLANT-CELLS SEQUENCE CLEAVAGE SITES THIOL PROTEASE TRANSGENIC TOBACCO YEAST VACUOLE0ZSProaleurain Vacuolar Targeting Is Mediated by Short Contiguous Peptide Interactions Plant Cell4p3307-318C Mar0 3270jdHolzenburg, A. Jones, P.C. Franklin, T. Pali, T. Heimburg, T. Marsh, D. Findlay, J.B.C. Finbow, M.E. 1993ELECTRON-MICROSCOPY GAP JUNCTION STRUCTURES HIGHER-PLANT MOLECULAR-CLONING PROTEOLIPID SUBUNIT QUATERNARY STRUCTURE SACCHAROMYCES-CEREVISIAE VACUOLAR H+-ATPASE VESICLE PROTON PUMP X RAY DIFFRACTIONpF@Evidence for a Common Structure for a Class of Membrane Channels& European Journal of Biochemistry 2131- 21-30 1 Apr<6Homma, T. Yoshihisa, T. Kihara, A. Akiyama, Y. Ito, K. 1995vpIntracellular stability of alpha fragments of beta-galactosidase: Effects of amino-terminally fused polypeptides:3Biochemical and Biophysical Research Communications 2152452-458&Homma, T. Yoshihisa, T. Ito, K.  1997xqSubunit Interactions in the Escherichia coli Protein Translocase: SecE and SecG Associate Independently with SecY FEBS Letters 408 11-15 n r   :   n V l 2357Freire, E. Snyder, B. 1980#COMPUTERS. LIPID BILAYERS. MATHEMATICS. MOLECULAR CONFORMATION GOV'T, P.H.S. THERMODYNAMICS #PHOSPHATIDYLCHOLINES. SUPPORT, U.S. GOV'T, NON-P.H.S. SUPPORT, U.SZSEstimation of the lateral distribution of molecules in two-component lipid bilayerso Biochemistry191 88-94e 8 Jane 2350D>Freire, E. Bach, D. Correa-Freire, M. Miller, I. Barenholz, Y. 1980`YCALORIMETRY, DIFFERENTIAL SCANNING. CEREBROSIDES/IP [ISOLATION AND #GLUCOSYLCERAMIDES/IP [ISOLATION AND PURIFICATION]. GLUCOSYLCERAMIDES HUMAN. KINETICS. SPLEEN/AN [ANALYSIS]. STRUCTURE-ACTIVITY RELATIONSHIP #PURIFICATION]. CEREBROSIDES. GAUCHER'S DISEASE/ME [METABOLISM] SUPPORT, U.S. GOV'T, NON-P.H.S. SUPPORT, U.S. GOV'T, P.H.S THERMODYNAMICSS^XCalorimetric investigation of the complex phase behavior of glucocerebroside dispersions Biochemistry1916 3662-3665 5 Aug 2359Freire, E. Snyder, B. 1982#COMPUTERS. LIPID BILAYERS/AN [ANALYSIS]. MATHEMATICS. MEMBRANE P.H.S PROTEINS/AN [ANALYSIS]. MONTE CARLO METHOD. SUPPORT, U.S. GOV'TbngQuantitative characterization of the lateral distribution of membrane proteins within the lipid bilayeraBiophysical Journal373617-624 Mar 235481Freire, E. Markello, T. Rigell, C. Holloway, P.W.a 1983|uCalorimetric and fluorescence characterization of interactions between cytochrome b5 and phosphatidylcholine bilayersN Biochemistry227b 1675-1680  29 MarB;Freire, E. van Osdol, W.W. Mayorga, O.L. Sanchez-Ruiz, J.M. 1990XQCalorimetrically determined dynamics of complex unfolding transitions in proteins<5Annual Review of Biophysics and Biophysical Chemistry19159-188 2360 2355Freire, E. Murphy, K.P. 1991~xACIDS DENATURATION DISSOLUTION GLOBULAR PROTEIN HISTIDINE HYDROPHOBIC INTERACTION MYOGLOBIN RIBONUCLEASE STABILITY WATER:4Molecular Basis of Co-operativity in Protein Folding 2223687-698 5 Dec-"Journal of Molecular Biology 2356NGFreire, E. Murphy, K.P. Sanchezruiz, J.M. Galisteo, M.L. Privalov, P.L. 1992COLD DENATURATION DIPHTHERIA-TOXIN DISSOLUTION GUANIDINE-HYDROCHLORIDE HYDROPHOBIC INTERACTION MYOGLOBIN SEQUENCE SURFACES THERMAL-STABILITY TRANSITIONThe Molecular Basis of Cooperativity in Protein Folding - Thermodynamic Dissection of Interdomain Interactions in Phosphoglycerate Kinase Biochemistry311250-256y 14 Jan 2353&Freire, E. Haynie, D.T. Xie, D.F 1993COOPERATIVITY FOLDED APOMYOGLOBIN INTERMEDIATE FOLDING INTERMEDIATES HYDROPHOBIC INTERACTION ORGANIZATION PROTEIN FOLDING PROTEIN THERMODYNAMICS RESOLUTION STABILITYhbMolecular Basis of Cooperativity in Protein Folding .4. CORE - A General Cooperative Folding Model172t111-123 Oct0*Proteins: Structure, Function and Genetics 2349 Freire, E. 1993`YStructural thermodynamics: prediction of protein stability and protein binding affinities.'Archives of Biochemistry and Biophysicss 303`2i181-184i Jun@ 2361JCFremont, D.H. Matsumura, M. Stura, E.A. Peterson, P.A. Wilson, I.A. 1992~xANTIBODY ANTIGEN-BINDING SITE HISTOCOMPATIBILITY ANTIGEN HLA-A2 HLA-B27 MOLECULES RECEPTOR RESOLUTION T-CELL RECOGNITIONXQCrystal Structures of 2 Viral Peptides in Complex with Murine MHC Class-I H-2K(b)8Science  257 5072919-927  14 AugFrenkel, L. Bremer, H. 1986f_Increased amplification of plasmids pBR322 and pBR327 by low concentrations of chloramphenicol. DNA5 6539-544 SJE 2362>7Frenken, L.G.J. Degroot, A. Tommassen, J. Verrips, C.T. 1993vpAERUGINOSA CIS-TRANS ISOMERASE CLONING ESCHERICHIA-COLI EXPRESSION INVIVO OUTER-MEMBRANE PROTEIN SIGNAL-SEQUENCE`YRole of the lipB Gene Product in the Folding of the Secreted Lipase of Pseudomonas-GlumaehMolecular Microbiology93591-599- Aug s5r,$q^/op(nm" 4048@9Komiyama, N.H. Shih, D.T.B. Looker, D. Tame, J. Nagai, K. 1991@:ESCHERICHIA-COLI EXPRESSION HEMOGLOBIN MYOGLOBIN SEQUENCESRKWas the Loss of the D-Helix in alpha-Globin a Functionally Neutral MutationS Nature 352 6333349-351A 25 Jul 4049,%Kondo, K. Kowalski, L.R.Z. Inouye, M. 1992BACTERIAL RIBOSOMES ESCHERICHIA-COLI HEAT NUCLEOTIDE-SEQUENCE RIBOSOMAL-RNA GENES SACCHAROMYCES-CEREVISIAE SMALL NUCLEAR-RNA SMALL NUCLEOLAR RNA TRANSLATION INITIATION U3TNCold Shock Induction of Yeast NSR1 Protein and Its Role in pre-rRNA Processing&Journal of Biological Chemistry 26723 16259-16265 15 Aug0*Konermann, L. Collings, B.A. Douglas, D.J. 1997aCytochrome c folding kinetics studied by time-resolved electrospray ionization mass spectrometry.      Biochemistry36 5554-5559 SJE 4051Konno, T. Morishima, I. 1993$LIGAND-BINDING PROTEINS SALTSTMEffects of Magnesium Sulfate on an Unfolding Step of Human Cyanomet MyoglobinDBiophysical Journal 652O907-911N Aug 4050Konno, T. Morishima, I. 1993BINDING GLOBULAR-PROTEINS GUANIDINE-HYDROCHLORIDE DENATURATION MODEL MYOGLOBIN UNFOLDING PROTEIN DYNAMICS PROTEIN STABILITY SOLVENT DENATURATION SPERM WHALE TRANSITION PATHWAY TRANSITION-STATE UREA HATransition State of an Unfolding Step in Human Cyanomet Myoglobinr$Biochimica et Biophysica Actao 1162 1-20 93-98 5 MarRLKonno, T. Kamatari, Y. O. Tanaka, N. Kamikubo, H. Dobson, C. M. Nagayama, K. 2000A partially unfolded structure of the alkaline-denatured state of pepsin and its implication for stability of the zymogen-derived protein Biochemistry3914 4182-4190PAlkylating Agents Animal Enzyme Precursors Enzyme Stability Pepsin A/*chemistry/metabolism Protein Denaturation *Protein Folding\Vhttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://dx.doi.org/10.1021/bi991923d20213270 SJE 4052(!Kono, K. Nishii, H. Takagishi, T.. 1993*$ACIDIC AMINO ACID ALPHA-HELIX AMINOISOBUTYRIC-ACID AMPHIPATHIC PEPTIDE AMPHIPHILIC POLYPEPTIDE ANTIMICROBIAL ACTIVITY CIRCULAR-DICHROISM CRYSTAL-STRUCTURE HYDROPHOBICITY INFLUENZA-VIRUS HEMAGGLUTININ LIPID BILAYER MEMBRANE-FUSION PH-DEPENDENCE PHOSPHOLIPID-VESICLES SMALL UNILAMELLAR VESICLESFusion Activity of an Amphiphilic Polypeptide Having Acidic Amino Acid Residues - Generation of Fusion Activity by alpha-Helix Formation and Charge Neutralization$Biochimica et Biophysica ActaH 11641t 81-90 24 Jun2+Kono, H. Nishiyama, M. Tanokura, M. Doi, J.P 1998bDesigning the hydrophobic core of Thermus flavus malate dehydrogenase based on side-chain packing " 0 Protein Engineering111 47-52 JAHd 4053.(Konrat, R. Burghardt, I. Bodenhausen, G. 1991LFEXCITATION INVERSION NMR CORRELATION SPECTRA PULSES SPIN SYSTEMS TOCSYXQNew NMR techniques are described for transferring transverse magnetization between scalar-coupled nuclei in the rotating frame. The methods involve simultaneous spin-locking of two selected spins A and X, using cosinusoidal modulation of the radio frequency (rf) carrier. If transverse magnetization of spin A is excited selectively before spin-locking, for example with a self-refocusing 270-degrees Gaussian pulse, in-phase magnetization will be transferred from spin A to spin X, and in-phase multiplets are obtained in both one- and two-dimensional spectra. The method allows one to verify whether two particular spins are connected by a scalar coupling. Examples are shown for peptides and basic pancreatic trypsin inhibitor (BPTI). The fine structure of the multiplets yields information on couplings to further spins. In contrast to nonselective spin-lock experiments, the magnetization cannot diffuse to a manifold of coupling partners. If relayed coherence transfer is to be achieved deliberately, several spins may be locked simultaneously by imposing an additional modulation on the rf carrier.tvpCoherence Transfer in Nuclear Magnetic Resonance by Selective Homonuclear Hartmann-Hahn Correlation Spectroscopy.(Journal of the American Chemical Society 113p24 9135-9140 20 Nov$Konrat, R. Yang, D. Kay, L.E. 1999tA 4D TROSY-based pulse scheme for correlating 1HNi,15Ni,13Cai,13C'i-1 chemical shifts in high molecular weight, 15N,13C,2H labeled proteinso .  / 1 @2 3  5 6 @7 8  : ; @< @= >  @ B @E p  r t  v x  y "Journal of Biomolecular NMRa15309-313  4054 Kontinen, V.P. Sarvas, M. 1993ALPHA-AMYLASE GENE AMYLOLIQUEFACIENS ESCHERICHIA-COLI SECB EXPORT EXPRESSION IDENTIFICATION MOLECULAR-CLONING PLASMA-MEMBRANE SERINE PROTEINASE TRANSLOCATION SYSTEM|vThe PrsA Lipoprotein Is Essential for Protein Secretion in Bacillus-Subtilis and Sets a Limit for High-Level SecretionMolecular Microbiology8P4e727-737i May0 CHEMICALly  e0 ey eQ e ep e e! e% e1% e[ e5 e7& e8 e e& e  e eO e e e#z o$| o+a o% o'O o0 o5 o6@ o7 o7 o7 o82 oo8^eelll l(llll-lllml l8l l-l.l/l-l1b'l2'l2'l2'l2'l4'l4'l12'l5'l6g'l6z'l6'l6'l7'l8D'l8a'l8y'l8'l8'l luminescencet$t7'schee6 tries7 yYy O Op O O< O  O ON O O= OR O O O$ O, O. O0R O/ O5 O6. O8  O9 O98 O9I O9Y O O O O O  O O, ON O O= OR O O O$ O O O O O  OODVCTB,A@ >= 58392+Overhoff, B. Klein, M. Spies, M. Freudl, R.G 19914-BACILLUS ESCHERICHIA EXPORT GENE PROTEIN SECApA DNA fragment that codes for the 364 N-terminal amino acid residues of a putative B. subtilis SecA homolog was cloned using the Escherichia coli secA gene as a probe. The deduced amino acid sequence showed 58% identity to the N-terminus of the E. coli SecA protein. A DNA fragment which codes for 275 N-terminal amino acid residues of the B. subtilis SecA homolog was expressed in E. coli, and the corresponding gene product was recognized by anti-E. coli SecA antibodies. This polypeptide, although only .apprx.30% the size of the E. coli SecA protein, also restored growth of E. coli MM52 (secAts) at the non-permissive temp., and the translocation defect of proOmpA in this mutant was relieved to a substantial extent. 0026-8925cIdentification of a gene fragment which codes for the 364 amino-terminal amino acid residues of a SecA homolog from Bacillus subtilis: further evidence for the conservation of the protein export apparatus in gram-positive and gram-negative bacteria 2283417-423$Juelich W-5170, Fed. Rep. Ger.$Molecular and General Genetics("Overhoff-Freundlieb, B. Freudl, R. 1991d^Suppression of an Escherichia coli secAts mutant by a gene cloned from Staphylococcus carnosus FEMS Microbiology Letters842143-149dJuelich W-5170, Germany  58412+ESCHERICHIA GENE MUTANT SECA STAPHYLOCOCCUSE. coli mutant MM52 (secAts) was transformed with a cosmid library from S. carnosus, and a recombinant cosmid (pBO23) allowing growth at the non-permissive temp. (42.degree.) was isolated. Plasmid pBO23 also restored the growth defects of E. coli mutants IQ85 (secYts) and IT41 (lepts). Nucleotide sequencing revealed that the DNA fragment responsible for the suppression effect codes for a S. carnosus protein highly homologous to the ribosomal protein L13 of E. coli. The staphylococcal L13 protein was efficiently incorporated into E. coli ribosomes. Possible explanations for the effect of this polypeptide on the growth of temp.-sensitive E. coli secretion mutants are discussed. 0378-1097 5842.(Owen, M.C. Beresford, C.H. Carrell, R.W. 1988Antithrombin Glasgow, 393 Arg to His: a P1 reactive site variant with increased heparin affinity but no thrombin inhibitory activity FEBS Letters 2312i317-320t 25 Apr 5843PJOwen, M.C. Shaw, G.J. Grau, E. Fontcuberta, J. Carrell, R.W. Boswell, D.R. 1989VOMolecular characterization of antithrombin Barcelona-2: 47 arginine to cysteinebThrombosis Research 554.451-457 15 AugOwen, D.J. Evans, P.R. 1998XRA structural explanation for the recognition of tyrosine-based endocytotic signalsSciencei 282 1327-1332 5844Ownby, D.W. Gill, S.J. 1990LFNonlinear optical effects in oxygen-binding reactions of hemoglobin A0Biophysical Chemistry37 1-3 395-406 31 Aug 5845:4Oyama, F. Shimada, H. Oyama, R. Titani, K. Ihara, Y. 1992@:AGED BRAIN ALZHEIMERS-DISEASE ALZHEIMERS-DISEASE BRAIN BETA-AMYLOID PROTEIN PRECURSOR MESSENGER RNA CHROMOSOMAL LOCALIZATION CORE PROTEIN DIFFERENTIAL EXPRESSION GENETIC-LINKAGE ISOFORM MESSENGER-RNA MICROTUBULE-ASSOCIATED PROTEIN NEUROFIBRILLARY TANGLES PAIRED HELICAL FILAMENTS TAU- MESSENGER RNA TRANSGENIC MICEztA Novel Correlation Between the Levels of beta-Amyloid Protein Precursor and tau-Transcripts in the Aged Human Brain Journal of Neurochemistryn593 1117-1125 SepS 5846&Ozaki, K. Itoh, N. Kawasaki, T.c 1993LECOATED PITS DOMAIN ENDOCYTOSIS GLYCOPROTEINS LYSOSOMES PROTEIN SIGNALRole of Tyrosine-5 in the Cytoplasmic Tail of the Macrophage Asialoglycoprotein Receptor in the Rapid Internalization of LigandsJournal of BiochemistryN 113I30271-276 Mar `6ItO7%47/47:47D47K47]47`47a47b47c47h47j47s47x47y47z47474747474747474747474747474747474747474747474747474848 4848448848948:48;48=48?48C48E48L48T48b48i48j48o48z48{484848484848484848484848484848484845'46u'48'4>41aair!bk9[kUkuraee8|lics+Yy43'e4a'e5'e6u'e6'e7'e7'e7'e8M'e8^'e8'e8'eerative  o'4u6'4>41aairb!kUkuraeeY+lya34'ea4'e5'eu6'e6'e7'e7'e7'eerative  o8660%1%1%22%3 3%43 0883 3130214749674@4%505%6%6 70768%8%8%97 243"3*3%G3%3+3105;00%0%1%3%213%4%46c666S6 6x66666%&65z555556r56565657_5757575)H5+h5+i5+k5+l5)F55%66- 7%71780848%88%8%9,Ofc,N,N,N,N,NN,N,N,N,N,N,N3NNoN#NN$xN>NXNNNON,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N+N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,N,NP:INTEractSyi!Gi"i#ai#i'i+i1@i ii?ii)icii xii?i^iiiii)$i*ioi i i#0i#zi#{i)i)+i)-i+iisi+si0i58i5i5i6i65i6?i6Oi6ei6fi6pi6xi6i6i7ui7we7~e7e7e85e8@e8Fe8Je8Pe8fe8|e8e8e8e7vedi7 i8 iingATIONgZTThe Escherichia coli secA gene, whose translation is responsive to the proficiency of protein export within the cell, is the second gene in a three-gene operon and is flanked by gene X and mutT. By using gene fusion and oligonucleotide-directed mutagenesis techniques, we have localized this translationally regulated site to a region at the end of gene X and the beginning of secA. This region has been shown to bind Se5TUtorial5t5t5t5t5t6t6t6t6/t62t66t6?t6Lt6mt6ot6t6t6t6t6t6t6t6t6t6t6t6t7t7t7t7!t7$t7%t79t7:t7=t7@t7Dt7Ft7Ht7Rt7kt7t7t7t7t7t7t7t7t7t7t7t7t7t7t7t8t8t8t8t8t!aG0KG0NGG=G 1`@ | endogenouslyelucanasey y3 y y  ywycanase,osidase METRIOSIS D y ycetalespnucleasee. p p p"R p&b p peptidase X l l) l% l66 s6 s7 s8E s/ s3&l4yl6Ol6l6l6l7l7l7l7l8l83l,lasmice5 e R R R R] R  # Analytical%[ z% z%  z+ z+< z* z- z z  z.y z.z z. z. z/ z/ z/ z0( z03 z06 z0 z0 z4 z  z z z z+y z6 z6 z6J z6{ z6 z7` z7j z7 z7 z7 z8 z8  z8G z8v z8 z7j' z/zed/dnd"Md5d6Hd6`d6ad6d6d7d7d8Nd8ddnFn$un$yn/n0i+iRole in Receptor-G-Protein Couplingn&Journal of Biological Chemistry 26830 22273-22276 25 OctCytopl Ҭ< 53050)Morjana, N.A. McKeone, B.J. Gilbert, H.F. 1993:3BONDS CATALYSIS DEPENDENCE MECHANISM RIBONUCLEASE-A Guanidine Hydrochloride Stabilization of a Partially Unfolded Intermediate During the Reversible Denaturation of Protein Disulfide Isomerase906 2107-2111 15 MarVOProceedings 7HX, UK. s.buchanan@mail.cryst.bbk.ac.ukBuchanan, S. K.@:99380826 0959-440x Journal Article Review Review, TutorialCurr Opin Struct BiolBacterial Outer Membrane Proteins/*chemistry Carrier Proteins/chemistry Crystallography, X-Ray Iron/metabolism Models, Molecular Phospholipases A/chemistry *Protein Conformation Protein Folding Receptors, Virus/chemistry Support, Non-U.S. Gov'tlehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=10449368 Evolution V V3 V V$5 V$ V%. V+ V V] V V V V V0 VX V | V / V  V - V  V C V  V  V V V V Vy V V Vg V V> V V V V V V V V V V V V V V  V! V" V# V#, V#Y V# V# V# V$ V$ V$ V%. V% V% VAtPa a Pa za!Fa!Ma!a!a!a!a!a"+a"1a"Ya"_a"ba"a#ea#za#{a#~a#a$a$qa$a%a& a&a&a&a&a&a]aha-|a a6a8ia7aa8aCaaOah11 1110171^111 a1 m1 1 1 p1A1E11)1 1 1 Ockner, R.K. Bass, N.M. Gordon, J.I.s 1984JDCloning of a cDNA encoding rat intestinal fatty acid binding protein812e313-317d JanVOProceedings of the National Academy of Sciences of the United States of AmericaD>Altamirano, M.M. Golbik, R. Zahn, R. Buckle, A.M. Fersht, A.R. 1997@:Refolding chromatography with immobilized mini-chaperones.94 3576-3578 SJEVOProceedings of the National Academy of Sciences of the United States of America,fS,gc,kc,pc,rc,tc(c+c&c,vc,xc,c,c,c,c,c,c*c*wc,c,c,c,cWcVcc,c,c,c9c,c,cc#c,c,c,c,c,c,c,c,c,c,c,c,c,c,c,c,c,c-c+c+c- ccclc-c-c-c-c-c-cNon of the SRP-SRP receptor complex. 1059-1524  UNITED STATESAnimal Binding Sites Dogs Endoplasmic Reticulum Guanosine Triphosphate Hydrolysis In Vitro M hp@ D1992226356609777783ACIDSAMINO AnalysisBiologyContact Coordination DimensionalG Galaktionov GLOBULARHYDROPHOBICITYin INTERIORM Matrices MolecularNumbersof PEPTIDES PREDICTION Proteins PROTEINSResidue RodionovSSepSITES StructureSURFACETerms i hЫ  ilibrium fluctuations in lipid bilayer systems from the excess heat capacity functionP$Biochimica et Biophysica ActaE 514i1 54-68 4 Deca 2358Freire, E. Snyder, B. 1980xq#COMPUTERS. LIPID BILAYERS. MATHEMATICS. MOLECULAR CONFORMATION #PHOSPHATIDYLCHOLINES. SUPPORT, U.S. GOV'T, P.H.SSb\Monte Carlo studies of the lateral organization of molecules in two-component lipid bilayers$Biochimica et Biophysica Actae 6003c643-6540 14 Aug $ # " ! j  :    2394PIFuhlendorff, J. Johansen, N.L. Melberg, S.G. Thogersen, H. Schwartz, T.W. 1990BETA-ENDORPHIN CIRCULAR-DICHROISM DESIGN DIMETHYL SULFIDE HORMONE MODEL PEPTIDES RECEPTOR-BINDING SECONDARY STRUCTURES SYNTHETIC PEPTIDES X-RAYptnThe Antiparallel Pancreatic Polypeptide Fold in the Binding of Neuropeptide-Y to Y1-Receptors and Y2-Receptors&Journal of Biological Chemistry2 265-20 11706-11712  15 Jul 2395D>Fujii, G. Horvath, S. Woodward, S. Eiserling, F. Eisenberg, D. 1992AMPHIPATHIC HELIX ENVELOPE GLYCOPROTEIN HTLV-III HUMAN IMMUNODEFICIENCY VIRUS HYDROPHOBIC MOMENT INFLUENZA-VIRUS LIPID BINDING MELITTIN MEMBRANE-FUSION OLIGOMERIC STRUCTURE PROTEIN MEMBRANE INTERACTIONS TRANSMEMBRANE PROTEIN TYPE-1ngA Molecular Model for Membrane Fusion Based on Solution Studies of an Amphiphilic Peptide from HIV gp41CProtein Science0111 1454-1464 Nov 2396,%Fujii, G. Selsted, M.E. Eisenberg, D. 1993AMPHIPATHIC PEPTIDE ANTIMICROBIAL PEPTIDES DEFENSINS DIRECT INACTIVATION LIPID BILAYER-MEMBRANES LIPID BINDING LIPID PEPTIDE INTERACTIONS MELITTIN MEMBRANE-FUSION NATURAL PEPTIDE ANTIBIOTICS NEUTROPHIL DEFENSIN PHOSPHOLIPID-MEMBRANES RABBIT GRANULOCYTES RESONANCE ENERGY-TRANSFER HBDefensins Promote Fusion and Lysis of Negatively Charged MembranesProtein ScienceH28 1301-1312 Aug 2397LFFujii, Y. Okamuro, y Hitotsubashi, S. Saito, A. Akashi, N. Okamoto, K. 1994*#ENTERO-TOXIN STB STRUCTURE ACTIVITYzsEffect of Alterations of Basic Amino Acid Residues of Escherichia coli Heat-Stable Enterotoxin II on enterotoxicityPInfection and Immunity62 2295-2301 239860Fujiinakata, T. Ishimi, Y. Okuda, A. Kikuchi, A. 1992yACID CHROMATIN COMPLEXES DNA H-3 IDENTIFICATION INVITRO MAMMALIAN-CELLS NEWLY SYNTHESIZED HISTONES XENOPUS-LAEVIS OOCYTES0Functional Analysis of Nucleosome Assembly Protein, NAP-1 - The Negatively Charged COOH-Terminal Region Is Not Necessary for the Intrinsic Assembly Activity&Journal of Biological ChemistryR 267r29 20980-20986 15 Oct 2399Fujiki, M. Verner, K. 1991{BOUND CYTOPLASMIC POLYSOMES CELLS INSERTION MEMBRANES MICROSOMES OUTER PRECURSOR TRANSLATION SYSTEM TRANSLOCATION TRANSPORTTb[Coupling of Protein Synthesis and Mitochondrial Import in a Homologous Yeast Invitro System &Journal of Biological Chemistrye 26611 6841-6847m 15 Apr 2400Fujiki, M. Verner, K. 1993ACCUMULATE MASSIVE AMOUNTS BOUND CYTOPLASMIC POLYSOMES CELLS DIHYDROFOLATE-REDUCTASE ENERGY-DEPENDENT UPTAKE INVITRO SYSTEM POST-TRANSLATIONAL IMPORT PRECURSOR POLYPEPTIDES SACCHAROMYCES-CEREVISIAE TRANSLOCATION~Coupling of Cytosolic Protein Synthesis and Mitochondrial Protein Import in Yeast - Evidence for Cotranslational Import Invivo&Journal of Biological Chemistryp 2683 1914-1920 25 Jan 2401JDFujimoto, I. Ikenaka, K. Kondo, T. Aimoto, S. Kuno, M. Mikoshiba, K. 1991BEE VENOM BREAKDOWN HIPPOCAMPUS LONG-TERM POTENTIATION MASTOPARAN MEMBRANE PERTUSSIS TOXIN RELEASE SYNAPTIC TRANSMISSION WASP VENOMrkMast Cell Degranulating (MCD) Peptide and Its Optical Isomer Activate GTP Binding Protein in Rat Mast Cells FEBS Letters 287 1-2 15-18 5 AugB;Fujimura, M. Kamakura, T. Inoue, H. Inoue, S. Yamaguchi, I. 1992Sensitivity of Neurospora crassa to Benzimidazoles and N-Phenylcarbamates - Effect of Amino Acid Substitutions at Position 198 in beta-Tubulin,%Pesticide Biochemistry and Physiology443165-173 Nov 2402ngASPERGILLUS-NIDULANS CLONING FUNGICIDES GENE IDENTIFICATION MUTAGENESIS MUTANT STRAINS RESISTANCE YEAST 240381Fujishige, A. Smith, K.R. Silen, J.L. Agard, D.A.r 1992~wEXPRESSION GENE HISTIDINE OUTER-MEMBRANE PEPTIDE BORONIC ACID PRECURSOR PRO-REGION PROTEINS SERINE PROTEASE SPECIFICITY0piCorrect Folding of alpha-lytic Protease Is Required for Its Extracellular Secretion from Escherichia-ColidJournal of Cell Biology8 118i1 33-42 Jult %4%%z%j%%^%%%%h% 8700<5York, D.M. Darden, T.A. Pedersen, L.G. Anderson, M.W. 1993ASPARTIC PROTEASE BINDING FREE-ENERGIES COMPLEX FORCE-FIELD HUMAN IMMUNODEFICIENCY VIRUS-1 INHIBITOR NUCLEIC-ACIDS PROTEINS RESOLUTION TYPE-1 PROTEASE}Simulations of the unbound form of the human immunodeficiency virus type 1 protease have been carried out to 200 ps in a crystalline environment and in solution. Solution simulations were performed with and without charge-balancing counterions. The results are compared with the 2.8-angstrom crystallographic structure of Wlodawer et al. [(1989) Science 245, 6161, and a proposed model for the solution structure which involves local refolding of the flap regions is presented. The simulations suggest the crystal packing environment of the protease dimer stabilizes the flaps in an extended conformation. Solvation of the dimer leads to local refolding of the flaps which contract toward the active site, forming increased overlap and stronger intersubunit hydrogn bonding at the tips. The degree to which the flaps overlap in solution is observed to depend on the charge state of the system.b\Molecular Dynamics Simulation of HIV-1 Protease in a Crystalline Environment and in Solution Biochemistry326 1443-1453 16 Feb 8702PIYoshida, K. Shibata, T. Masai, J. Sato, K. Noguti, T. Go, M. Yanagawa, H. 1993NGAQUEOUS-SOLUTION CONFORMATION H 1 NMR IMMUNODOMINANT SITE PEPTIDE UNITSBvoProtein Anatomy - Spontaneous Formation of Filamentous Helical Structures from the N-Terminal Module of Barnasea Biochemistry329  2162-2166m 9 Mar 8701Yoshida, H. Ihara, Y. 1993ALZHEIMERS-DISEASE BRAIN CDNA EPITOPES EXPRESSION FETAL-TAU ISOFORMS MICROTUBULE-ASSOCIATED PROTEIN MICROTUBULES PAIRED HELICAL FILAMENT-TAU PAIRED HELICAL FILAMENTS PHOSPHORYLATION SEQUENCES TUBULIN~tau in Paired Helical Filaments Is Functionally Distinct from Fetal tau - Assembly Incompetence of Paired Helical Filament-tau Journal of Neurochemistryn613w 1183-1186a SepoYoshida, M. Amano, T.t 1995F@A common topology of proteins catalyzing ATP-triggered reactions 3598 1-2  1-5n FEBS Letters 8703F?Yoshihara, Y. Nagase, H. Yamane, T. Oka, H. Tani, I. Higuti, T.A 1991ANISOTROPIC INHIBITORS BETA D THIOGLUCOSIDE BOVINE HEART-MITOCHONDRIA CHARGERIN-II A6L COUPLING FACTOR-B ENERGY TRANSDUCTION HYDROPHOBIC PROTEIN MEMBRANE-PROTEINS NONIONIC DETERGENT OXIDATIVE-PHOSPHORYLATION SYSTEMH+-ATP Synthase from Rat Liver Mitochondria - A Simple, Rapid Purification Method of the Functional Complex and Its Characterization Biochemistry3028 6854-6860 16 Jul 8704,&Yoshihisa, T. Barlowe, C. Schekman, R. 1993zsADP-RIBOSYLATION FACTOR BINDING-PROTEIN CLONING CYTOPLASM ER FUSION MECHANISM RAS PROTEINS TRANSPORT VESICLES YEASTd]Requirement for a GTPase-Activating Protein in Vesicle Budding from the Endoplasmic ReticulumScience 259 5100 1466-1468 5 MarYoshihisa, T. Ito, K.i 1996Pro-OmpA derivatives with a His(6) tag in their N-terminal ''translocation initiation domains'' are arrested by Ni2+ at an early post-targeting stage of translocation 27116 9429-94365&Journal of Biological Chemistry  8706*$Yoshikawa, K. Aizawa, T. Hayashi, Y. 1992CARCINOMA CELL-LINE DIFFERENTIATION DISEASE DOWNS-SYNDROME EXPRESSION LOCALIZATION MESSENGER-RNA MICROGLIA PEPTIDE SENILE PLAQUESjdDegeneration In vitro of Post-Mitotic Neurons Overexpressing the Alzheimer Amyloid Protein Precursor Nature 359c 6390 64-67 3 Sep 8705PIYoshikawa, H. Jeong, S.M. Hirata, A. Kawamura, F. Doi, R.H. Takahashi, H.0 1993jdESCHERICHIA-COLI EXPORT EXPRESSION HOMOLOGY INITIATION MEMBRANE PROTEIN SEQUENCE SPO0A TRANSLOCATION`YTemperature-Sensitive Sporulation Caused by a Mutation in the Bacillus-Subtilis secY GeneJournal of Bacteriology 17511 3656-3660 Jun 8707NGYoshimori, T. Semba, T. Takemoto, H. Akagi, S. Yamamoto, A. Tashiro, Y. 1990|ANTIBODY BINDING-PROTEIN LOCALIZATION LUMINAL ER PROTEINS MEMBRANE PEPTIDE SECRETION SEQUENCE TRANSFERRIN RECEPTOR TRANSPORTProtein Disulfide-Isomerase in Rat Exocrine Pancreatic Cells Is Exported from the Endoplasmic Reticulum Despite Possessing the Retention Signal&Journal of Biological Chemistry 265r26 15984-15990 15 SepD>Yoshimune, K. Yoshimura, T. Nakayama, T. Nishino, T. Esaki, N. 2002|LHsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli < :3Biochemical and Biophysical Research Communications 29351389-95. May 2412054669:4Adenosinetriphosphatase/metabolism Alanine/chemistry Amino Acid Motifs Amino Acid Sequence Amino Acids/chemistry Bacterial Proteins/*physiology Cloning, Molecular Dose-Response Relationship, Drug Escherichia coli/*metabolism Escherichia coli Proteins/*physiology Glutamic Acid/chemistry Heat-Shock Proteins/*physiology Heat-Shock Proteins 70/*physiology Histidine/chemistry Molecular Chaperones/*physiology Molecular Sequence Data Mutation Plasmids/metabolism Proline/chemistry Protein Binding Protein Structure, Tertiary Sequence Homology, Amino Acid Time Factorseng Journal ArticleF'XQInstitute for Chemical Research, Kyoto University, Uji, Kyoto-Fu 611-0011, Japan. 87094-Yoshimura, T. Noguchi, H. Inoue, T. Saito, N.  1991F@CONFORMATION GENERAL-CONSIDERATIONS MOLTEN-GLOBULE STATE PATHWAYB;Mechanism of Protein Folding .2. Lysozyme and PhospholipaseIBiophysical ChemistryN403h277-291e JulD. Furcht, L.T.. 1993ADHESION ATTACHMENT BINDING DOMAIN CORNEA EPITHELIUM FIBRONECTIN HEPARAN-SULFATE PROTEOGLYCANS HUMAN-PLASMA FIBRONECTIN IDENTIFICATION III CONNECTING SEGMENT MIGRATION MONOCLONAL-ANTIBODY MOTILITY SITE-DIRECTED MUTAGENESIS SURFACECharacterization of FN-C/H-V, a Novel Synthetic Peptide from Fibronectin That Promotes Rabbit Corneal Epithelial Cell Adhesion, Spreading, and Motility.341U153-164R Jan4.Investigative Ophthalmology and Visual Science1ZPOSTi1[a1\a1]a1^a1_a1`a1aa1ba1ca1da1ea1fa1ga1ha1ia1ka1la1ma1na1oa1pa1qa1ra1sa1ta1ua1va1wa1xa1ya1za1{a1|a1}a1~a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1a1ae Scripps Research Institute, Department of Molecular Biology and Skaggs Institute for Chemical Biology, 10550 North Torrey Pines Road, La Jolla, CA, 92037, USA..11090279 J Mol Biol 2000 3043d355-70.ZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11063572:NHHuntley, J. J. Scrofani, S. D. Osborne, M. J. Wright, P. E. Dyson, H. J.yDynamics of the metallo-beta-lactamase from Bacteroides fragilis in the presence and absence of a tigh ;B : 8 9 7 6 5G. 1992ATPH CHLOROPLAST GENOME CHROMOPHYTA ESCHERICHIA-COLI EXPORT GENE ORGANIZATION INSERTION NUCLEOTIDE-SEQUENCE OPERON PAVLOVA-LUTHERII PROTEIN TRANSLOCATION PROTEIN TRANSLOCATION ATPASE SEE-Y SIGNAL-SEQUENCE SUBUNITS SYNTHASECharacterisation of a Chloroplast-Encoded sec-Y Homologue and atpH from a Chromophytic Alga -Evidence for a Novel Chloroplast Genome Organisation FEBS Letters 304S 2-3119-123 15 Jun 6890~ 7433>7Spangler, B.D. Heerze, L.D. Clark, C.G. Armstrong, G.D. 1993~wADHERENCE AFFINITY-CHROMATOGRAPHY BORDETELLA-PERTUSSIS CARBOHYDRATE-RECOGNITION DOMAINS CELL MODEL PURIFICATION SUBUNITOVOHydrophobic Binding of Pertussis Toxin Is Enhanced by Oligosaccharide Receptorsn.'Archives of Biochemistry and Biophysics  305t1153-158 15 Aug 7435B Model Peptides and Their Conformational Analysis<5International Journal of Peptide and Protein Research40 3-4h322-332-Sep-Oct3N  Freskgard1992 Freskgard1993, Freskgard1995t Freudl19879; Freudl19909> Freudl1991e= Freudl19919" Freudl19929# Freudl19939% Freudl19939 Freudl1993 # Freudl19950 Freudl200007 Freudl200007 Freudl200118T Freudl2003kJ Freund19939  Freund1993 + Freund1995%1 Freund1996 ,x Freund19963 Freund19966& Freund1997 ) Freund19988,k Freund19988-O Freund19999.B Freund19999. Freund19999/ Freund20002n Freund200103 Freund200204' Freund200225 Freund200309H Frey198219G Frey198339F FREY1985+` Frey19869  Frey1990v Frey19909  Frey1991v Frey19922 Frey19922 Frey19939)E Freyman1996 Freymann1990IFreymann19933 Freymann1997*Freymann19980Freymann19990Freymann200001Freymann20011Freymann200104 Freymann2002y4$Freymann20027Freymann20027Freymann2002y8Freymann2004y? Freyssinet1993 Friboulet1993 Fric19901# Frickel2002 Friden1991 U Fridkin1990V Fridkin1993 Fridkin1993%Fridland1994( Fridovich1982-F Fridricksson1999/ Fridriksson2000/ Fridriksson2000 Fried1991 Fried1993 Friedberg1993 Frieden1988 Frieden1988& Frieden1988& Frieden1988  Frieden1988 Frieden1989 m Frieden1989 M Frieden1989 Frieden1990  Frieden1990 Frieden1990& Frieden19918 Frieden1991 Frieden1992 Frieden1992 } Frieden1992 Frieden1992 Frieden1993  Frieden1993,: Frieden1994  Frieden1995 Frieden1995F Frieden1996 Frieden1996( Frieden1997( Frieden1997& Frieden1997+; Frieden1998+ Frieden1998,; Frieden1998. Frieden1998, Frieden1999, Frieden19992 Frieden20011 Frieden20022 Frieden20024 Frieden20025 Frieden2003  Friederich1992Friedman1991Friedman1992 Friedman1992Friedman19929xFriedman1993$Friedman19939Friedman1993Friedman1993$JFriedman1993 Friedman19933 W Friedrich19936 Friedrich2001* Friedrichs11988  Friedrichs1991  Friedrichs1992  Friedrichs19933) Friedrichs19955+ Friedrichson19985B Friel20038 Friel20044 Frien20028D Frien2003  Friend1994 0 Friesen1999Friesner199497Friesner2001l Frigerio1993 Friguet1988  Friguet1989 = Friguet1990  Friguet1990 Friguet1991 Friguet1992 Frings1993 ) Frings1995 Frisch19811,u Frisch19979,| Frisch19972m Frisch2001</(Frishman1999 Fritsch1982w Fritsch19898# Fritsch1989 Fritz1993 Fritz199483 Fritz2003 Frobe1993 Frobert19931 Froebe19931}Frohlich1991gFrohnert1992& Froland19968p Froloff2002 Frolow1994G Fromm1993  Frommel1989  Frommel1990Fronczek1990 Fronczek1993  Fronticelli1993 Frosch19921 Frosch199313 Frderberg2002 Frutiger1993 Fry1992 Fry1992 Fry1992 Fry1993 Fry1993 Frydman1992  Frydman1992  Frydman1994/  Frydman19971| Frydman19991} Frydman19999= Frydman1999/ Frydman20001I Frydman20011\ Frydman20017 Frydman20019< Frydman20017 Frydman20027 Frydman20037 Frydman20037 Frydman2003,1 Frye1996  Fu1991  Fu19923 Fu20012 Fuchs1967 Fuchs1967 Fuchs1967  Fuchs1967  Fuchs19671995t Freudl19879; Freudl19909> Freudl1991e= Freudl19919" Freudl19929# Freudl19939% Freudl19939 Freudl1993 # Freudl19950 Freudl200007 Freudl200007 Freudl20011J Freund19939  Freund1993 + Freund1995%1 Freund1996 ,x Freund19963 Freund19966& Freund1997 *~ Freund19988) Freund19988,k Freund19988-O Freund19999.B Freund19999. Freund19999/ Freund20002n Freund200103 Freund200204' Freund200225 Freund20030+` Frey19869  Frey1990v Frey19909  Frey1991v Frey19922 Frey19922 Frey19939)E Freyman1996 Freymann1990IFreymann19933 Freymann1997*Freymann19980Freymann19990Freymann200001Freymann20011Freymann200104 Freymann2002y4$Freymann20027Freymann20027Freymann2002y? Freyssinet1993 Friboulet1993 Fric19901# Frickel2002 Friden1991 U Fridkin1990V Fridkin1993 Fridkin1993%Fridland1994( Fridovich1982-F Fridricksson1999/ Fridriksson2000/ Fridriksson2000 Fried1991 Fried1993 Friedberg1993 Frieden1988 Frieden1988& Frieden1988& Frieden1988  Frieden1988 Frieden1989 m Frieden1989 M Frieden1989 Frieden1990  Frieden1990 Frieden1990& Frieden19918 Frieden1991 Frieden1992 Frieden1992 } Frieden1992 Frieden1992 Frieden1993  Frieden1993,: Frieden1994  Frieden1995 Frieden1995F Frieden1996 Frieden1996( Frieden1997( Frieden1997& Frieden1997+; Frieden1998+ Frieden1998,; Frieden1998. Frieden1998, Frieden1999, Frieden19992 Frieden20011 Frieden20022 Frieden20024 Frieden20025 Frieden2003  Friederich1992Friedman1991Friedman1992 Friedman1992Friedman19929xFriedman1993$Friedman19939Friedman1993Friedman1993$JFriedman1993 Friedman19933 W Friedrich19936 Friedrich2001* Friedrichs11988  Friedrichs1991  Friedrichs1992  Friedrichs19933) Friedrichs19955+ Friedrichson19985B Friel20035 Friel20034 Frien2002  Friend1994 0 Friesen1999Friesner1994 Frigerio1993 Friguet1988  Friguet1989 = Friguet1990  Friguet1990 Friguet1991 Friguet1992 Frings1993 ) Frings1995 Frisch19811,u Frisch19979,| Frisch19972m Frisch2001</(Frishman1999 Fritsch1982w Fritsch19898# Fritsch1989 Fritz1993 Fritz19948% Fritz2004 Frobe1993 Frobert19931 Froebe19931}Frohlich1991gFrohnert1992& Froland1996 Frolow1994G Fromm1993  Frommel1989  Frommel1990Fronczek1990 Fronczek1993  Fronticelli1993 Frosch19921 Frosch199313 Frderberg2002 Frutiger1993 Fry1992 Fry1992 Fry1992 Fry1993 Fry1993 Frydman1992  Frydman1992  Frydman1994/  Frydman19971| Frydman19991} Frydman19997 Frydman1999/ Frydman20007 Frydman20001I Frydman20011\ Frydman20017 Frydman20017 Frydman20017 Frydman20017 Frydman20027 Frydman20037 Frydman20037 Frydman2003,1 Frye1996  Fu1991  Fu19923 Fu20012 Fuchs1967 Fuchs1967 Fuchs1967  Fuchs1967  Fuchs1967s1967VTRSQP0NOLMKpJ--,wItH 7210f`Shoemaker, K.R. Fairman, R. Schultz, D.A. Robertson, A.D. York, E.J. Stewart, J.M. Baldwin, R.L. 1990HASide-chain interactions in the C-peptide helix: Phe 8 ... His 12+o Biopolymerso291 1-11 Jan` 7214"Shoemaker, M.T. Haley, B.E.r 1993\UACTIVATION AMINO-ACID SEQUENCE ATP BRAIN GUANOSINE 5'-TRIPHOSPHATE IONS LEUCINE LIVER Identification of a Guanine Binding Domain Peptide of the GTP Binding Site of Glutamate Dehydrogenase -Isolation with Metal-Chelate Affinity Chromatography2 Biochemistry327 1883-1890 23 Feb,&Shoemaker, B.A. Wang, J. Wolynes, P.G. 199782Structural correlations in protein folding funnelsVOProceedings of the National Academy of Sciences of the United States of America94777-782  JAHd$Shoemaker, B.A. Wolynes, P.G.d 1999jdExploring structures in protein folding funnels with free energy functionals: The denatured ensemble"Journal of Molecular Biology 287657-674d JAH,&Shoemaker, B.A. Wang, J. Wolynes, P.G. 1999rkExploring structures in protein folding funnels with free energy functionals: The transition state ensemble\"Journal of Molecular Biology 287675-694d 7215Shoji, M. Golde, T.E. Ghiso, J. Cheung, T.T. Estus, S. Shaffer, L.M. Cai, X.D. McKay, D.M. Tintner, R. Frangione, B. Younkin, S.G. 1992}ADRDA WORK GROUP CLINICAL-DIAGNOSIS CRITERIA DEGRADATION DISEASE FRAGMENTS LOCALIZATION PEPTIDE PRECURSOR SOLUBLE DERIVATIVESeXQProduction of the Alzheimer Amyloid-beta Protein by Normal Proteolytic ProcessingScience 258 5079126-129 2 Octg 72166/Shon, K.J. Kim, Y.G. Colnago, L.A. Opella, S.J.n 1991BACTERIORHODOPSIN MICELLES MODEL N-15 CHEMICAL-SHIFT PHOTOSYNTHETIC REACTION CENTER RESOLUTION SOLID-STATE SPECTROSCOPY TENSORSG`ZNMR Studies of the Structure and Dynamics of Membrane-Bound Bacteriophage-Pfl Coat ProteinSciencei 252 5010 1303-1304l 31 May 7218Shore, D. Baldwin, R.L. 1983XQEnergetics of DNA twisting. I. Relation between twist and cyclization probability` 170 47957-981 15 Nov"Journal of Molecular Biology 7217Shore, D. Baldwin, R.L. 1983:3Energetics of DNA twisting. II. Topoisomer analysis 1704983-1007 15 Nov"Journal of Molecular Biology 7225Shortle, D. Botstein, D. 19830*Directed mutagenesis with sodium bisulfite 100h457-468rMethods in Enzymologyr 7219 Shortle, D. 1983>8A genetic system for analysis of staphylococcal nuclease Gene22 2-3181-189May-Jun 7233*#Shortle, D. Novick, P. Botstein, D. 1984piConstruction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene8115 4889-4893 AugVOProceedings of the National Academy of Sciences of the United States of America 7228Shortle, D. Lin, B. 1985Genetic analysis of staphylococcal nuclease: identification of three intragenic "global" suppressors of nuclease-minus mutationsGenetics 1104 539-555l Augp 7229Shortle, D. Meeker, A.K. 1986tnMutant forms of staphylococcal nuclease with altered patterns of guanidine hydrochloride and urea denaturation1l1 81-89 Sepe0*Proteins: Structure, Function and Genetics 7220 Shortle, D. 1986^WGuanidine hydrochloride denaturation studies of mutant forms of staphylococcal nuclease& Journal of Cellular Biochemistry304y281-289 7231*#Shortle, D. Meeker, A.K. Freire, E. 1988Stability mutants of staphylococcal nuclease: large compensating enthalpy-entropy changes for the reversible denaturation reaction Biochemistry2713 4761-4768 28 Jun 7230Shortle, D. Meeker, A.K. 1989leResidual structure in large fragments of staphylococcal nuclease: effects of amino acid substitutionsi Biochemistry283F936-944e 7 FebCRASSA OUTER-MEMBRANE PRECURSOR PROTEIN SIGNAL PEPTIDE YEAST MITOCHONDRIASpjBilayer-Penetrating Properties Enable Apocytochrome-c to Follow a Special Import Pathway into Mitochondria& European Journal of Biochemistry 204i2841-846. 1 Mar- 3661Jorgensen, W.L.6 1991JC3-DIMENSIONAL STRUCTURE ANTIBODY ANTIGEN COMPLEX PEPTIDE RESOLUTIONB2,F2*2&S2 2,J2,L2 2+2,Y2,[2*2,]2,_2F2,c2,g2,n2(2&2,v2,v2,v2,v2v,2,v2,v2,v2,v2'OH+laIa(aHa&a)Daa%7a aa+qa+a+a+a+a+a+a+a+a+a+a+a+a+a+a*a,aa,a*a, a*a*a(a(aa*a*a*a*eaa+@a+Ba, a, a)a,a*a a#<aFa)a,a+a+a+a+a+a+a+a+a+a+a"V"a*Va"a#a#@a#Va#ya#za#{a#|a#a#a#a#a#a#a$a*a$a$a+6a$a$a$a$a*Ea%!a%,a&a%Na%Oa%a%a&a&a&&a&(a&*a&+a&Wa&a)!a+]a+aa+ja+ka7a+a+a+a+a+a+a&a%1a+a+a+a+a+a+a+a#  resonance) p) p#P p#m p#u p# p# p# p# p# p# p# p# p# p# p# p$ p$0 p$: p$U p$g p$f p$j p$ p$ p$ p$ p% p%  p% p% p%) p%0 p%Z p%_ p%b p%g p%| p% p% p% p% p% p% p% p% p% p&  p&1 p&D p&C p&A p&A p&A p&A pA& p&A p&A p&A p&A p&A p&A p AnTibodies g g g g g^ g go g| g g` g g g? g gI g  g X g  g 5 g > g  g  g  g @ g~ g g g gC g g gj go g g gk g gb gx g gP g g g g g g gw g< g; g g g!J g#@ g% g&+ g g0 g0 g2 g g g g g g g g g^ g go g| g g` g g g? g gI g  gX  g  g5  g>  g@  g  g  g  g@  g~ g g g gC g g gj go g g gk g gb gx g gP g g g g g g gw g< g; g g gJ! g@# g% g+& g g g g gB"HLloveras ydM46'uis8M9Fb8H'blP >o6o*ama~aa0|a3&a4na7adeCedi'5ii.iiiDingCb7b]b-bachovR$u Rb-e17rrr8,rrtszssi7oiigsster c6caitoncliiii`i*i i i i5iiviuiiYiiii&iiAiMoltenlMWMM&M+MeMM(MEMMMHMNMbMgMM)MM gM M+M =M M M M M 3M M M4M6MMKMMMMMMMMMtMM6MMMM~MMbMbMbMbMbMbMgMgMgMgMgMgMgM+0Ofc,=N*N*N,>N,?N,AN+?N+N,CN+N,DN+EN&NdN,EN,FN*N\N,GN,HN,IN,JN,KN,MN,NN,ON,PN,QNN NoN,RN,SN N,UN,VN+N,WN,YN+N,[N,\N,]N,^N,_N,`NFN,aN*N)N)N,cN,dN,eN(N,fN,fN,fNf,N,fN,fN,fN,fN333000000r0q00 04000000|0~0000%0^00M0f00000*0!0!@0!i0!0"0"90"?0"0"0"0"0#0#0%{0%0&0+00,:0#I0,N0,R00.0,0,0,0,0,0,0,0,0ermodynamic transition tryptophanX9 9" 33ochemistry 9 9" 9492q33333 3**3^3333T33J3t3?3331333*3"3$ 3$3$3-R32-32C353535363833300 0 :0 0000d0c00 O0"0"0%#0, 0-0.0+z0/0100303030304F04E05M05L0Q0H00h000 0000B00000pson19799Thompson19809Thompson19811iThompson19811 Thompson19811+bThompson1985!Thompson1986!Thompson1989Thompson1990Thompson19909"Thompson1990Thompson19911Thompson19919Thompson19919 Thompson19911 Thompson19911!Thompson1991#ThompsonObbbbbbb %b @b wb b b b b!b!b!Cb!Ob!b!b"b"b"fb"b"b"b"b"b"b"b"b#*b#yb#|b#b#b#b$Ob$^b$nb${b$b%b%b%6b%b&b&-b&.b&/b&Ub&b&b)3b'Rbeb'Mb+b*bb(b,*bbC/C/C&C C/,C//C"C.C(C/:CsC',C/[C/yC/sC/hC,C/SC/C,bC- C- C-C,C+C.C.C/C.C/C/C/C(C/C/C/C/C/C/C/C/C/C/C/C/C/C/C/C`C$CD C C Ca C CC7C\Cccccc/kOfc/ln/un/vn/wn/xn/dn/Zn,n/Sn/n/n/{n-n-n,bn+zn- n-n,n,n,n.n.n. n.n.n.n.n.n+n+n+n+n+n-n.n.&n.(n.on.n.n.n.n.n..n-n/0n/n.n/n/n)nKn-Pn+n+tn+Yn+snnnnnnOremoverorrossYtt aJiri ing<gVATEdCing on eorei itiesyddd xyLy]yldatedIFdamsoditionallyE eNINEIyly ylimidodiphosphateJhesions}JuvantspPRenalsorptionvanceseExample 9changed|rr"r-/rdioi'1iing*tluded retiont'hibitedistence&rocytosisTOXINperimenta als ly  s% llainedo-oitsGorteee eds(-sedure,"resSednion F F  F / F t t t t( t t(ftendision '"t  racellulare'Tion$emeFaaa Ka wa aMau5555555]55f5555 21-30 1 Apr<6Homma, T. Yoshihisa, T. Kihara, A. Akiyama, Y. Ito, K. 1995vpIntracellular stability of alpha fragments of beta-galactosidase: Effects of amino-terminally fused polypeptides:3Biochemical and Biophysical Research Communications 2152452-458&Homma, T. Yoshihisa, T. Ito, K.  1997xqSubunit Interactions in the Escherichia coli Protein Translocase: SecE and SecG Associate Independently with SecY FEBS Letters 408 11-1564-3A!((`b*4Br+!"["#d$S%E&*n*e(, ,,,,9-)U $-,-U-a1-r1-s4-y, ---.;--.G.j...............[/n/5/o//.H0)0*-0*;1s1|12MN2S-($5 56n6677x7789-)U $-, ,Ande#e$e%e*e-e1e2e7e8e)e:e=e>eBeDeFeHeLeOeNe[e`e_e^e]ecedefe*jeieuexe{eeeeeeeeeeeeeeeeeeeeeeeeeeeeeeBRUM 266PJAvoustin, P. Mostachi, H. Perret, B. Cambou, J.P. Cambien, F. Depreval, C. 1992DENSITY LIPOPROTEIN RECEPTOR DNA DOMAIN FAMILIAL DEFECTIVE APOLIPOPROTEIN-B-100 GENE GRADIENT GEL-ELECTROPHORESIS HYPERCHOLESTEROLEMIA MUTATION POLYMERASE SEQUENCElztA Very Conservative Region of ApoB-100 in the Putative Binding Region to the LDL Receptor in the Toulouse PopulationHuman Genetics904.460-463 Dec Ӏ ܸ 261:4Aune, K.C. Sal1989#/9%979K99 008"00002000A00 L0 20 50R0}00+"0*0&000h0L0000#~0#0$#0$60$0%%0+H0,0/00M00203F0)00 c0,0K040000#00006E0800 0 11/1.1<1?1D1X1j1u1z1111111111111111*1,1Q1400000 0 11/1.1<1?1D1X1j1u1z1111111111111111*1,1Q1r1RESOLvedO31n36n3n3n5Pn6Wnnnnznnnnnn +n *nnnniiii8iiiiiiii#i$2i% ii]ii/iis,s!'s#s#Ls+ss69s6Is6Ws7s7s8us8s8sRsing& n) n6 n4n6Ba6Ya6a6a8Sa8xa8ya8a8a-aCanceS} S S S Snn+ n* nnnniiii8iiiiiiii#i2$i %ii]ii/iis,s'!s#sL#ss+s96sI6sW6sRsing& n) n4nB6aY6a-aCanceS} S S S S0 Baud199913 Baud2002D Z Baudier1992 Baudier1992'1 Bauer1991 Bauer1992 Bauer1992 Bauer1992< Bauer1994$R Bauer19947K Bauer2003 Bauerle1991 Bauerle1991, Bauerle1998 Bauernfeind1992 Baulieu1992 Baulieu1992 Baum1989vB Baum19909D Baum19919 Baum19922 Baum1992vc Baum19922. Baum19939 Baum19939I Baum19939 Baum1993vd Baum1993y5 Baum199335 Baum1997+ Baum1998v5 Baum19989-8 Baum1999x/k Baum19999/ Baum2000037 Baum20022 Baumann1991- Baumann1999' Baumeister1990  Baumeister1991 b Baumeister1992  Baumeister1992 h Baumeister1992 $ Baumeister1993 * Baumeister1997 < Baumert1993 Baumruk19939 Baur19959~ Baures1992 ,Bautista1998 Bautsch1993* Bavoso19889& Bax19854 Bax19854 Bax1986q Bax1988*m Bax1989* Bax1989* Bax1989 Bax1989 Bax1989 Bax1989 Bax1989 Bax1989s Bax1990v Bax1990 Bax1990 Bax1990 Bax1990 Bax1990 Bax1990 Bax1990P Bax1990S Bax1990R Bax1990Q Bax1990 Bax1990 Bax1990'[ Bax1991 Bax1991 Bax1991 Bax1991T Bax1991 Bax1991 ? Bax1991 > Bax19917 Bax1991 Bax1992 Bax1992 Bax1992 Bax1992# Bax1992# Bax1992 Bax1992 Bax1992 Bax1992 Bax1992  Bax1992 Bax1992 Bax1992 Bax1992) Bax1992, Bax1992 Bax1993 Bax1993# Bax1993# Bax1993# Bax1993# Bax1993 Bax1993  Bax1993  Bax1993$ Bax1993 Bax1993# Bax1993 Bax1994  Bax1996"% Bax1996*a Bax1997*% Bax1997* Bax1998. Bax1999. Bax1999. Bax1999. Bax1999/ Bax20001 Bax20011 Bax20013 Bax20024 Bax20028q Bax20027L Bax2003,d Baxa19979+ Baxter19929 Baxter19933 Baxter1993 + Baxter1997+ Baxter19980) Baxter1999 9a Baxter200529f Baxter2005r9k Baxter2005r Bayan1993 Bayer19903 Bayer2002 Bayerl1990  Bayerl1992  Bayerl19939 Bayley19922# Bayley1992r Bayley1996 ,7 Bayley1997s8z Bayley200208 Bayly1995 ! Bayne1992 Bazan1992 Bazinet1988 Bazinet1990 Bazzi1991P Bazzo1991%J Bazzo19914 Buml20034 Beach2002 Beal19919 Beall1987) Beals1991 Beamer1988) Beamer199596Q Beamer200006 Beamer20000 Bean19911~ Bean19929 Bean19921 Bean199212 Bean2002-7 Bear20030 Beard1993 Bearden1990! Bearden1992 Bearer19911  Beasley1992. Beasley19994E Beasley2002  Beattie1991 Beatty19939- Beauchamp1998- Beauchamp19988v Beauchemin20022"Beaulieu1992/ Beavil2000 Bebrin1993 $ Bech199312; Bechert2001Y Bechet1993  Bechinger1991 Bechinger1991 Bechinger19923Bechtold1992 Beck1990v, Beck19922 Beck19922 Beck1992v Beck19933# Beck19939 Beck1993v& Beck19939( Beck1997v, Beck199800 Beck20005 Beck20001 Beck200103} Beck20017 Beck200107 Beck2003010Beck-Sickinger1997U! Becka1990$ Becker19919 Becker19911 Becker1992 v Becker1993  Becker1993 Becker19933" Becker19949 Becker19969 Becker1996 / Becker2000r4 Becker20024 Becker2002 Beckers1993 Beckers1994$ Beckett1993 c Beckingham1993 & Beckingham1993 ' Beckman1992Beckmann1992Beckmann1993Beckmann1993*6Beckmann19977_Beckmann20017Beckmann2001 Becksickinger1993 Becktel1983L Becktel1987 Becktel19872 Becktel1988 Becktel1988$ Becktel19883 Becktel1989 Becktel1990 Becktel1992 Becktel1992Beckwith1978Beckwith1979Beckwith1979Beckwith1981eister1990  Baumeister1991 b Baumeister1992   Baumeister1992 h Baumeister1992 $ Baumeister1993 * Baumeister1997 < Baumert1993 Baumruk1993~ Baures1992 ,Bautista1998 Bautsch1993* Bavoso19889& Bax1985q Bax1988m* Bax1989* Bax1989 * Bax1989 Bax1989 Bax1989 Bax1989 Bax1989 Bax1989s Bax1990v Bax1990 Bax1990 Bax1990 Bax1990 Bax1990 Bax1990 Bax1990P Bax1990S Bax1990R Bax1990Q Bax1990 Bax1990 Bax1990[' Bax1991 Bax1991 Bax1991 Bax1991T Bax1991 Bax1991? Bax1991> Bax1991 Bax1992 Bax1992 Bax1992 Bax1992# Bax1992# Bax1992 Bax1992 Bax1992 Bax1992 Bax1992 Bax1992 Bax1992 Bax1992 Bax1992) Bax1992, Bax1992 Bax1993 Bax1993# Bax1993# Bax1993# Bax1993# Bax1993 Bax1993 Bax1993 Bax1993$ Bax1993 Bax1993# Bax1993 Bax1994 Bax1996%" Bax1996a* Bax1997%* Bax1997* Bax1998. Bax1999. Bax1999. Bax1999. Bax1999/ Bax20001 Bax20011 Bax2001d, Baxa19979+ Baxter19929 Baxter19933 Baxter1993 + Baxter1997+ Baxter1998)0 Baxter1999  Bayan1993 Bayer1990 Bayerl1990  Bayerl1992  Bayerl19939 Bayley19922# Bayley1992r Bayley1996 7, Bayley1997s! Bayne1992 Bazan1992 Bazinet1988 Bazinet1990 Bazzi1991P Bazzo1991J% Bazzo1991 Beal19919 Beall1987) Beals1991 Beamer1988) Beamer19959 Bean19911~ Bean19929 Bean19921  Bean19921 Beard1993 Bearden1990! Bearden1992 Bearer19911 Beasley1992. Beasley1999 Beattie1991 Beatty19939- Beauchamp1998- Beauchamp1998"Beaulieu1992/ Beavil2000 Bebrin1993 $ Bech19931Y Bechet1993  Bechinger1991 Bechinger1991 Bechinger19923Bechtold1992 Beck1990v, Beck19922 Beck19922 Beck1992v Beck19933# Beck19939 Beck1993v& Beck19939( Beck1997v, Beck199800 Beck20001 Beck2001001Beck-Sickinger1997U! Becka1990$ Becker19919 Becker19911 Becker1992 v Becker1993  Becker1993 Becker19933" Becker19949 Becker19969 Becker1996 / Becker2000r Beckers1993 Beckers1994$ Beckett1993c  Beckingham1993 & Beckingham1993 ' Beckman1992Beckmann1992Beckmann1993Beckmann19936*Beckmann1997 Becksickinger1993 Becktel1983L Becktel1987 Becktel19872 Becktel1988 Becktel1988$ Becktel19883 Becktel1989 Becktel1990 Becktel1992 Becktel1992Beckwith1978Beckwith1979Beckwith1979Beckwith19811#c6#b#a#`#_#^ 8150.(Verbon, A. Hartskeerl, R.A. Kolk, A.H.J. 1991AMINO-ACID ANTIGENIC STRUCTURE B-CELL EPITOPES BOVIS BCG DIFFERENT CONFORMATIONS ESCHERICHIA-COLI HEAT-SHOCK PROTEIN LEPROSY MONOCLONAL-ANTIBODIES MYCOBACTERIUM-TUBERCULOSIS PEP SCAN PREDICTION PULMONARY TUBERCULOSIS SEQUENCECThe human immune response to the 10-kD M. tuberculosis protein was studied by a competition ELISA using monoclonal antibody (MoAb) SA-12. Twenty-five per cent of the sera from 20 patients with tuberculosis and none from 21 control subjects inhibited binding of SA-12 to the 10-kD antigen. To characterize the antigenic parts of the 10-kD antigen, overlapping decapeptides according to the amino acid sequence of the 10-kD protein were synthesized. In total, 91 sequential decapeptides, with an overlap of nine amino acids, were tested in ELISA with MoAb SA-12, human and murine sera (PEP scan). SA-12 recognized the amino acid sequence WDEDGEK (amino acid 50-56). All human sera, from patients with tuberculosis as well as from control subjects, gave almost identical undulating patterns of reactivity with the decapeptides. No relationship was found between the ability of the patients' sera to inhibit binding of MoAb SA-12 and the binding of these sera to the decapeptides comprising the epitope recognized by SA-12 in the PEP scan. Apparently, antibodies in patients' sera against the 10-kD protein are predominantly directed against discontinuous epitopes and, consequently, the continuous epitopes as presented in the PEP scan are not suitable to discriminate between patients with tuberculosis and control subjects. In the PEP scan, sera from BALB/c mice, both non-immunized and immunized with either live M. tuberculosis or the 10-kD protein gave similar patterns of reactivity, albeit different from the patterns obtained with the human sera. However, after immunization of the mice, clearly increased levels of antibodies to primary structures of the 10-kD protein were observed.C}Murine and Human B-Cell Epitope Mapping of the Mycobacterium-Tuberculosis 10-kD Heat Shock Protein Using Overlapping PeptidesS*$Clinical and Experimental Immunology861y 6-12 Oct 8151VOVerbon, A. Hartskeerl, R.A. Schuitema, A. Kolk, A.H.J. Young, D.B. Lathigra, R.s 1992~w65-KILODALTON ANTIGEN BOVIS DNA ESCHERICHIA-COLI EXPRESSION GENE LEPRAE LEPROSY MONOCLONAL-ANTIBODIES SEQUENCE-ANALYSISThe 14,000-Molecular-Weight Antigen of Mycobacterium-Tuberculosis Is Related to the Alpha-Crystallin Family of Low-Molecular-Weight Heat Shock ProteinsuJournal of Bacteriologys 174 4 1352-1359 Febt 815282Verdaguer, N. Perello, M. Palau, J. Subirana, J.A. 1993ALPHA-HELIX CHROMATIN CIRCULAR-DICHROISM CONFORMATION HISTONE H-1 ORGANIZATION POLYPEPTIDES PROTAMINES SECONDARY STRUCTURE SPERMZTHelical Structure of Basic Proteins from Spermatozoa -Comparison with Model Peptides& European Journal of Biochemistry 2143879-887 15 Jun 81530)Verdini, A.S. Chiappinelli, L. Zanobi, A. 1991HACHAIN IMMUNOGENICITY INVITRO PEPTIDES SECONDARY STRUCTURE SPECTRAiToward the Elucidation of the Mechanism of Attachment and Entry of Malaria Sporozoites into Cells -Synthetic Polypeptides from the Circumsporozoite Protein of Plasmodium-Falciparum Bind Ca2+ and Interact with Model Phospholipid Membranes1 Biopolymers7316587-594 May8 8154Vergeres, G. Waskell, L. 1992BINDING CROSS-LINKING EMBEDDED SEGMENT INSERTION LIVER MICROSOMAL CYTOCHROME-P-450 MUTAGENESIS PHOTOACTIVATABLE PHOSPHOLIPIDS PROTEINS PURIFICATION REDUCTASEngExpression of Cytochrome-b(5) in Yeast and Characterization of Mutants of the Membrane-Anchoring Domaina&Journal of Biological Chemistryr 26718 12583-125917 25 Jun 8155:3Verheyden, P. Francq, W. Pepermans, H. Vanbinst, G. 1990f_DIMETHYLSULFOXIDE H 1 NMR POTENT REDUCED RING SIZE SMS 201-995 SPECTRA SPECTROSCOPY SUPPRESSIONNGConformational Study of a Somatostatin Analogue in DMSO/Water by 2D NMRo Biopolymersa30 7-8855-860SMall E    !!%!_!"d#$$%/&C+,W,_.,,'-4*,-q--."-H.&//s///)/111112b2334f4e)$(566n66688898)mkLoZl,  &)nq4 G @EJ9:u !#0)Di!u+p#|'//7~m8Q)J9:u !#0)Di!u+p#).Rutkats.6o7ogowski!e y l7 l&ledge&Lter2uskav'vinov. y.!y( ysschaertK v v& v v# z66 z(zza)diger,v2l1jl1Vl2egsegger+0licke)+ved)W+zy7F'etzel2XRvwyabov&-lls&.n]nnqzrzz)z*z+zz,Sz14o6o6o1(odinezantsev2 D8bakDBERG,e-pf/4f7ffTffelN-kowskiT-leN  NGKETLQRA.pniewskiser}tka/u6VEVoynanen54<'z5'e eszotarskaS SSIcccc ccc(ccccc#c*c+c/c0c1c2c4c5c9c;c>c?c@cAcFcc9c;c>c?c@cAcFcc (,4/ ) n96036764$Aboul-ela, F Karn, J Varani, G|vThe structure of the human immunodeficiency virus type-1 TAR RNA reveals principles of RNA recognition by Tat protein. 253o2d 313-32 1995:3MRC Laboratory of Molecular Biology, Cambridge, UK.The human immunodeficiency virus type-1 (HIV-1) Tat protein stimulates transcriptional elongation. Tat is introduced to the transcription machinery by binding to the transactivation response region (TAR) RNA stem-loop encoded by the 5' leader sequence found on all HIV-1 mRNAs. We have used multidimensional heteronuclear NMR to determine the structure of the TAR RNA in the presence of the ADP-1 polypeptide, a 37-mer that carries the minimal RNA recognition region of the Tat protein and closely mimics Tat binding specificity. In the presence of a variety of ligands, including ADP-1, related basic peptides and the amino acid derivative argininamide, the bulge region of TAR undergoes a local conformational rearrangement and forms a more stable structure. The structure of TAR in the bound form has been determined from over 1000 NMR-derived constraints. The U23 residue at the 5' end of the bulge is positioned near G26 and A27 in the major groove, rather than stacked on A22 as in the free TAR. U23 and G26 are brou ght into close proximity by contacts to the guanidinium group and side-chain amide group of a common arginine residue. However, the interaction of this guanidinium group with TAR is not the only source of binding specificity. Besides NOEs to the arginine residue participating in the conformational change, ADP-1 shows additional intermolecular NOEs to TAR, suggesting that there are multiple points of contacts between TAR RNA and residues from the basic and core regions of Tat. These structural results provide important clues towards the identification of small molecular mass and/or peptidomimetic inhibitors of the essential Tat-TAR interaction. 0022-2836 ENGLANDAmino Acid Sequence Bacterial Proteins Base Sequence Binding Sites Comparative Study Exons Gene Products, tat Human Hydrogen Bonding HIV-1 Ligands Membrane Proteins Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance Nucleic Acid Conformation Oligoribonucleotides Protein Conformation RNA, Viral Sequence Homology, Amino Acid Support, Non-U.S. Gov't Transcription, Genetic"Journal of Molecular Biology13Abraham, F.F. Kardar, M. 1991f_CRUMPLING TRANSITION DYNAMICS FLUCTUATIONS POLYMERIZED MEMBRANES STATISTICAL-MECHANICS SURFACES>7Folding and Unbinding Transitions in Tethered MembranesUScienceS 252 5004419-422c 19 Apr60Abraham, J. Kelly, J. Thibault, P. Benchimol, S. 2000tnPost-translational modification of p53 protein in response to ionizing radiation analyzed by mass spectrometry"Journal of Molecular Biology 2954853-864Amino Acid Sequence Electrophoresis, Polyacrylamide Gel Human Leukemia, Myelocytic, Acute Molecular Sequence Data Peptide Fragments/chemistry/isolation & purification Phosphorylation Phosphoserine/analysis Protein p53/*chemistry/*metabolism/radiation effects Protein Isoforms/chemistry/metabolism/radiation effects Protein Processing, Post-Translational/*radiation effects Radiation, Ionizing Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Support, Non-U.S. Gov't Tumor Cells, Culturedtnhttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.idealibrary.com/links/citation/0022-2836/295/85320123976 SJE<5Abrahams, J.P. Leslie, A.G.W. Lutter, R. Walker, J.E. 1994D=Structure at 2.8 of F1-ATPase from Bovine Heart Mitochondria Nature 370 621-628P14 F1-ATPASE CRYSTALLOGRAPHYe16Abrams, F.S. London, E. 1992BILAYERS CYTOCHROME-B5 FATTY-ACID MODEL MEMBRANES N-(7-NITROBENZ-2-OXA-1,3-DIAZOL-4-YL)-LABELED LIPIDS PHOSPHATIDYLCHOLINE PROBES VESICLESCalibration of the Parallax Fluorescence Quenching Method for Determination of Membrane Penetration Depth - Refinement and Comparison of Quenching by Spin-Labeled and Brominated Lipids Biochemistry3123 5312-5322 16 Jun150)Abrams, F.S. Chattopadhyay, A. London, E. 1992}DEPENDENCE DISPERSIONS ENERGY-TRANSFER ESR FLUIDITY GRADIENT LECITHIN LIPID BILAYER MEMBRANE PROBES TRANSVERSE PLANE VESICLESDetermination of the Location of Fluorescent Probes Attached to Fatty Acids Using Parallax Analysis of Fluorescence Quenching - Effect of Carboxyl Ionization State and Environment on Depth Biochemistry3123 5322-53273 16 JunHAAckermann, E.J. Ang, E.T.-H. Kanter, J.R. Tsigelny, I. Taylor, P.  1998Identification of pairwise interactions in the alpha-neurotoxin-nicotinic acetylcholine receptor complex through double mutant cycles&Journal of Biological Chemistry 273H18 10958-10964 JAHP@:Acquotti, D. Bonomi, F. Brocca, P. Ganadu, M.L. Pagani, S. 1994Some Structural Features of Cluster-Coordinating Cysteines of Clostridium Pasteurianum are Revealed by 2D TOCSY 1H NMR on the Oxidized Protein > V p  q :3Biochemical and Biophysical Research Communications 2021591-595 SJE26 Adams, M.D. Oxender, D.L. 1991AMINO-ACID SUBSTITUTION CLEAVAGE SITE EXPORT IMMUNOGLOBULIN LIGHT-CHAINS MALTOSE-BINDING MATURE LAMB OUTER-MEMBRANE PERIPLASMIC PROTEIN SECONDARY STRUCTURE SIGNAL-SEQUENCEhaSecretion of Mutant Leucine-Specific Binding Proteins with Internal Deletions in Escherichia-Colin& Journal of Cellular Biochemistry464321-330 Aug25Adams, B. Lerner, L. 1992 NMRxqWe have measured temperature coefficients of the chemical shifts, scalar coupling constants, and exchange rates for the hydroxyl protons in sucrose in mixtures of water and acetone. The values measured are virtually the same for all the hydroxyl protons in sucrose. These observations indicate that there are no persistent hydrogen bonds in sucrose in aqueous solution.CyObservation of Hydroxyl Protons of Sucrose in Aqueous Solution - no Evidence for Persistent Intramolecular Hydrogen Bonds .(Journal of the American Chemical Society 114 12 4827-4829 3 Junin, S. Wetlaufer, D.B. Rose, G. Hopkins, T.E. 1975.'Library currently receives this journalF?Minimization of construction errors in bent-wire protein models  Biopolymers-143633-640r Mar, 2673VPGoldberg, M.E. Semisotnov, G.V. Friguet, B. Kuwajima, K. Ptitsyn, O.B. Sugai, S. 1990tnAn early immunoreactive folding intermediate of the tryptophan synthease; beta 2 subunit is a 'molten globule' FEBS Letters 2631u 51-56f 9 Apr` VCannot &orooo1o6o6o6o6po6o6o77o7|o7o8o8oonicalt8 t8 t) t) t6 t6 t6 t7 t8 ttersl"l#l0ini'/ley'.o+o*0o8'oblanco&r'o-o/A oo(p)p*p"P6&pepa aa$$a+Nava~a a3I3]3 33"M3536M3 327)73 abilitiesB y5 y6  y y l% l+Y l6& l'leCCCXC$C5CCC CC+ CC#ClCC#zC)'C'MC0C6C7#C7C7C8TC8C CITANCE  I I ICCXCC)'CC CC+ C'MCC#ClCC CITANCE  I I IoIESd$o3$1$1$1$1%1%1&1&1+1 K1+11*1U1,1,1*1,%1*1*1*1,L1*1,1,1*1q1!;1!:1,1*11#x1 s1/ 11$1/11J1^1-]1+1+31(1,1111U11\11_11`111212~121)11)1 14141516<16s161617H1718181819I19J1&1'11*1U1,1,1*1,%1*1*1*1,L1*1,1,1*1q1!;1!:1,1*11#x1 s1/ 11$1/11J1^1-]1+1+31(1,1111U11\11_11`111212~121)1141)1 1&1'11gh`7pUniqueg7l7l7l7l7l7l83l88l8l8l8l8l8l8l4lyn6Mn8,n8nn,nesst-4 t) tteeeeEe$te-e/e6eee e\eiee ee e qee#e#e0e6-e6Se6Te6e6e8ze)e2'e4I'e4g'e6a'e6'e6'e8'e3'e3'd4b'd73'dd V>pMpVsnsrs&swszsteeeeEet$e-e/e/e6eee e\eie/ee ee eq ee#e#e0e-6eS6eT6e6e6e)e2'eI4'eg4'ea6'e6'e6'e3'e3'db4'd37'dd V>pMpVsnsrs&swszssB.&Academy.(n.on.n.n.n.n.n-n/0n/n/n#&n0 n0n0.n0Rn0rn0n0n0n0n0n#n1#nn1n)Qn1&n1!n/n0n0n1%n1n,n.n"n0~nnenn/n4}nn#n4nn4n4:n50n6n8n8n9 n9nj n0R n1@'n4'n4D'n4>'n4'n5x'n5~'n7#'n7'n7'n7'n nthamoebathamoeba0/n/n/n&#n 0n0n.0nR0nr0n0n0n0n0n0n#n#1nn1nQ)n&1n!1n/n0n0n%1n1n1n,n.n"n~0nnenn/n}4nn#n4nn4n:4n05nj nR0 n@1'n4'nD4'n>4'n4'nx5'n~5'n nthamoebaoebaVDass#tItaeeeeeeHekeeee Pe _e e e e~eeeeeTeeeeeee`eeeee e'ee*eeeee Ge e!e!e"re# e+e+e+e+e,/e e-!e Ce-e.e.e- eiee0e0e1e1e2Ge3je4le4e'Ze4e55e6%e6e7 e7de7e8e8e95e e+e)ee)BsBeeeieeee`ee eeeee e'ee*eeeee Ce Ge e!e!e"re)e# e'Ze+e+e+e e)ee)BsB7Gov't7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a8a8a8a8a8 a8a8a8a6a8$a8)a8,a8-a82a84a89a8:a8<a8?a8?a8?a8?a8?a8?a8?a8?a8?a8 s8 s8 s see6e6e8vee dee d a@ P developed iM iQ io i Y i#/ i+^ i+y i'Z i5 i6 i6# i6& i69 i6x i6{ i6~ i6 i6 i6 i7 i7 i77 i7I i7 i7 i7 i7 i7 i7 i8] i8j i8 i8 i8 i8 i8 i8 i8 i ing"r m$ m m! m# m INtracellular  d!" d"  d#3 d#M d#g d$p d$q d$ d$ d% d& d)) d d+i d+j d+k d)D d+{ d* d2 d5 d5 d6A d6p d7P d8D d8` d8 d- d2 d y  i i7 h h h5 l6 l6 l6L l6g l6 l6 l6 l7 l7 l7! l7$ l7) l7* l7> l7@ l7A l7a l7s l7 l7 l7 l7 l7 l m6 m7u m8{ s7u s7~ m merii3iIii%i0i0i1i~iikiiii_i6ni7;i7ci ict t t t  s s, s6n s s s0 z8 z% zations,ls-s6nss t  t[ t" t t  t6 T -THYLe ethylenediaminei%i~iikiiii_$Sep$$1$;e$?$Ee$O$`$c$j$n$$$%%9%H%^%\%a%s%t%}%%%%%%%%%&&D&>&Y&_&s&{&'''!+X p N t4,43474544414944UI&dopt=Citation&list_uids=10601012a 7799HATheriault, T.P. Leahy, D.J. Levitt, M. McConnell, H.M. Rule, G.S.n 1991yStructural and kinetic studies of the Fab fragment of a monoclonal anti-spin label antibody by nuclear magnetic resonanceS 221t1257-270l 5 Sep "Journal of Molecular Biology 7800lfTheriault, Y. Logan, T.M. Meadows, R. Yu, L.P. Olejniczak, E.T. Holzman, T.F. Simmer, R.L. Fesik, S.W. 1993HBSolution Structure of the Cyclospori7J7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a8a8a8a8 a8a8 a,a1a8a8a8a8a8a8a8 a8#a8$a8,a8.a80a82a82a82a82a82a82a82a82a82a82aProtein Folding Problemo8824 11076-11080 DecnVOProceedings of the National Academy of Sciences of the United States of Americat 3078<6Headgordon, T. Stillinger, F.H. Wright, M.H. Gay, D.M. 1992&CHARMM COMPUTER FOLDING PROBLEMjcPoly(L-alanine) as a Universal Reference Material for Understanding Protein Energies and StructuresF8923 11513-11517  1 DecpVOProceedings of the National Academy of Sciences of the United States of AmericaQ|$ Wild1992v$ Wild1992v$ Wild1992v$ Wild1993v$ Wild1996v6 Wild2000e1 Wild20011 Wild20028* Wild20032( Wildegger1997+ Wildegger1997) Wildegger1998- Wildegger19993f Wildegger1999 Wiles1993-~ Wiley1981+w Wiley1987  Wiley1990 Wiley1990  Wiley1991- Wiley1991 , Wiley1992 Wiley1992 Wiley1992 Wiley1992 Wiley1992+ Wiley1992 Wiley1993- Wiley19947 Wiley1995+ Wiley1998,} Wiley1998 Wilhelm1990= Wilhelm1993 X Wilk19931- Wilk19999 Wilkemounts1991, Wilkes19979V Wilkins1969I Wilkins1992$ Wilkins1993+" Wilkins1997* Wilkins1997/p Wilkins19990 Wilkins2000$3 Wilkinson1983$ Wilkinson1983$ Wilkinson1984% Wilkinson1984X Wilkinson1984 Wilkinson1985 Wilkinson1985 ; Wilkinson1985 : Wilkinson1985 Wilkinson1993$ Wilkinson1993$ Wilkinson1996* Wilkinson1997* Wilkinson19970_ Wilkinson1997+8 Wilkinson19986 Wilkinson20016 Wilkinson20011 Wilkinson20023 Wilkinson20028 Wilkinson2004^ Will19939Willaert19922*uWillbold1994 Wille1990$ Wille1992$ Wille1992$ Wille1992 Wille19930 Wille2001 Willems1993 Willems1993, Willems19982 Willems20021Y Willer20018N Willer2003 Willett1993.s Willett1997 Willey19855$ Willey1991 Williams19700- Williams19777Williams1985]Williams1988Williams19899$Williams1989Williams1989WWilliams1990VWilliams1990$Williams19909 Williams19909$8Williams1990#PWilliams1990$Williams1990%AWilliams1990 Williams1991YWilliams1991$Williams1991$Williams1991 Williams1991aWilliams1991yWilliams1991#Williams1991%CWilliams1991t%BWilliams1991Williams1991Williams1991t,Williams19922ZWilliams1992Williams1992Williams19929$Williams1992'Williams1992"Williams1992Williams19922Williams1992#Williams1992|Williams1992Williams1992Williams1992 Williams1993 Williams1993wWilliams1993vWilliams1993Williams19939Williams1993UWilliams1993oWilliams1993CWilliams1993@Williams19933Williams19939Williams1993Williams19933%DWilliams1993Williams1993Williams19947Williams1994$Williams1996)Williams19969'PWilliams1996*OWilliams1997)Williams19979)Williams19979+?Williams19989+qWilliams19988.Williams19993NWilliams2002w3Williams20024Williams2003: Williamson1984 f Williamson1989 $ Williamson1990 4 Williamson1990d ) Williamson19919  Williamson1991  Williamson1991 $ Williamson1992 $ Williamson1992 i Williamson1992 ) Williamson1993 &# Williamson1994  Williamson1996 ) Williamson1996 ( Williamson1997 * Williamson1998 + Williamson19981T Williamson2001/ Willie20002> Willimsky1993Willison1992'Willison1992Willison1993Willison1993Willison1993 Willison19939Willison1994%  Williston1989 R Wills1991 S Wills1992$ Wills19934b Willson20026 Willumeit2003$Wilmanns1993#xWilmanns1996-Wilmanns19999SWilmanns2004a& Wilmans1997$ Wilmot1988 $Wilsbach1993Wilschut19911Wilschut1993. Wilsher1996$ Wilson1977 $ Wilson1978 H Wilson19818-~ Wilson1981) Wilson1984 ) Wilson19858P Wilson1987 Wilson19877 Wilson19879 Wilson1990  Wilson19900 Wilson19909 Wilson1991  Wilson1991  Wilson19919 Wilson19919$ Wilson1991 $ Wilson1991 $ Wilson1991 1 Wilson1992 Wilson19929 Wilson1992 Wilson19929b Wilson1992e9 Wilson19929$ Wilson1992 $ Wilson1992 $ Wilson1992 Wilson19931 Wilson19933 Wilson19939!B Wilson1993 Wilson1993 "M Wilson19939 Wilson1993 % Wilson1993 Wilson19939b Wilson19931h Wilson1993e/ Wilson19930H Wilson19957 Wilson19959 V Wilson19966$ Wilson1996 0I Wilson199660Z Wilson1998<6 Wilson20006 Wilson2003 Wilting1993/s Wilton199996 Wilton19999 Q Wiltscheck1992 > Wiltscheck1993 g Wiltscheck199693/ Wiltsie2002*EWimberly19976Wimberly19972Wimberly1999X$ Wimley1992$ Wimley1993 ) Wimley1998  Winand199398 Winans1999 Winant1991 ; Winblad1991, Winchester1998'@ Winder19951( Winder1997 T Windsor1991)Winfield1990*Winfield1991$ Wing1991v' Winge1991% Winger1992 q Wingfield1988 Wingfield1989  Wingfield1989  Wingfield1989% Wingfield1989  Wingfield1989s Wingfield1990u Wingfield1990t Wingfield1990  Wingfield1990* Wingfield1990 Wingfield1990  Wingfield1991  Wingfield1991  Wingfield1991+} Wingfield1991 Wingfield1992#< Wingfield1993  Wingfield1996+ Wingfield1998. Wingfield19991 Wingfield2000,Wingreen1998% Wingren1996%$ Winiski19929I Winitz19611 P Winitz19922 Winkelmann19939%Winkfein1992+ Winkler1998+ Winkler19987Z Winkler1998/v Winkler19995 Winkler20026h Winkler20029V Winneker RC1990% Winning1992% Winsborrow1991 $3 Winter1983 $ Winter19839$ Winter19849% Winter1984X Winter1984  Winter19859 Winter19858 Winter1985o Winter19859 < Winter1985 ; Winter19859 : Winter19859 Winter1987 A Winter19889% Winter1990 / Winter1991 % Winter1991 G Winter1992 '= Winter19933 Winter19949. Winter19979- Winter19993 Winter20011) Winterhalter1993 W Wintermeyer1993 Wintermeyer1994 Wintermeyer1996* Wintermeyer1998, Wintermeyer19980 Wintermeyer19980 Wintermeyer20001 Wintermeyer20017u Wintermeyer2001% Winther1991+*Wintjens1998&4 Winyard1990%  Winyard1991 Winzor199098 Winzor200202 Wirmer20020 Wirth19925 Wirth19978D Wirth2003 Wirtz1990 ? Wirtz1991%  Wirtz1991 Wischik1990( Wischik1991= Wischik1991P Wischik19916 Wischik1992[ Wise19921 Wise19931 Wise1993 Wise19949t Wise19941s Wise19949%  Wiseman1989 Wiseman19937 Wiseman2003%  Wishart1991%  Wishart1991% Wishart1992% Wishart1993'Z Wishart1994% Wishart19947 Wishart19941 Wishart19955 Wishart19951 Wishart19981 Wishart20011 Wishart20021 Wishart2002 Wisnieski1986 Wisnieski1987l Wisnieski1988 Wisnieski1990se19949'Z Wishart1994% Wishart1995 Wisnieski1986 Wisnieski1987 Wisnieski19901990 f2J*u {|}& 4967Mayr, L.M. Schmid, F.X. 1993|vANION BINDING CONFORMATIONAL STABILITY DENATURATION FREE-ENERGY CHANGES LINEAR EXTRAPOLATION RIBONUCLEASE-A SALTS UREA82Stabilization of a Protein by Guanidinium Chloride Biochemistry3231 7994-7998 10 AugMayr, L.M. Schmid, F.X. 1993tnKinetic Models for Unfolding and Refolding of Ribonuclease-T(1) with Substitution of Cis-Proline-39 by Alanine"Journal of Molecular Biology 2313 913-926 5 Jun  4966CATALYSIS CIS FOLDING KINETICS FOLDING REACTIONS ISOMERIZATION MECHANISM PHASE PROLINE MODEL PROLYL CIS/TRANS-ISOMERIZATION PROLYL ISOMERASE PROTEIN FOLDING REPLACEMENT SMALL PROTEINSSJE JAH0*Mayr, L.M. Landt, O. Hahn, U. Schmid, F.X. 1993xStability and folding kinetics of ribonuclease-T1 are strongly altered by the replacement of cis-proline-39 with alanine 0 @1 ] ` "Journal of Molecular Biology 2313897-912 5 Jun 4965CIS TRANS ISOMERIZATION CONFORMATIONS FOLDING KINETICS ISOMERISM MECHANISM NMR OLIGOPEPTIDES PROLINE RESIDUES PROLINE SUBSTITUTION PROLYL CIS/TRANS-ISOMERIZATION PROTEIN FOLDING PROTEIN STABILITY PROTEINS SITE-DIRECTED MUTAGENESIS TRYPTOPHAN SYNTHASESJE JAH4.Mayr, L.M. Willbold, D. Rosch, P. Schmid, F.X. 1994?Generation of a non-prolyl cis peptide bond in ribonuclease T1   > @"Journal of Molecular Biology 240288-293 SJE JAH`81Mayr, L.M. Odefey, C. Schutkowski, M. Scmid, F.X.P 1996tmKinetic analysis of the unfolding and refolding of ribonuclease T1 by a stopped-flow double-mixing technique. Biochemistry35 5550-5561ESJE JAH 4968:4Mazodier, P. Guglielmi, G. Davies, J. Thompson, C.J. 1991ANTIGEN CLONING ESCHERICHIA-COLI GAMMA-SUBUNIT HEAT-SHOCK PROTEINS MYCOBACTERIUM-TUBERCULOSIS OPERON POLYMERASE-III HOLOENZYME PRODUCTS SEQUENCEThree GroEL-like heat shock proteins (HSP56, HSP58, and HSP18) have been observed in Streptomyces albus (G. Guglielmi, P. Mazodier, C. J. Thompson, and J. Davies, J. Bacteriol. 173:7374-7381, 1991). Here we report the cloning and complete nucleotide sequence of groEL1, which encodes HSP18 and HSP58, and groEL2, which encodes HSP56. Both nucleotide sequences predicted proteins of 56,680 Da that were 70% identical. The 5' nucleotide sequence of groEL1 coded for a protein corresponding to HSP18 that may be a processed gene product. At least two groEL-like genes were present in all 12 Streptomyces species tested; they were not closely linked in the genome. groEL1, but not groEL2, was adjacent to a groES-like gene.ID>Characterization of the groEL-Like Genes in Streptomyces-AlbusJournal of BacteriologyR 17322 7382-7386A Nov 4969Mazzoni, M.R. Hamm, H.E. 1993ADP-RIBOSYLATION AMINO-ACID SEQUENCE BETA-GAMMA CDNA SEQUENCE CHYMOTRYPSIN ELONGATION-FACTORS GT, TRANSDUCIN INTRINSIC FLUORESCENCE NUCLEOTIDE-BINDING PROTEIN PERTUSSIS TOXIN PROTEOLYSIS RAS ROD GTP-BINDING PROTEIN ROD OUTER SEGMENTSSTryptophan207 Is Involved in the GTP-Dependent Conformational Switch in the alpha-Subunit of the G-Protein Transducin - Chymotryptic Digestion Patterns of the GTP-gamma-S and GDP-Bound Forms"Journal of Protein Chemistry122o215-221c Apr 49706/McBride, H.M. Millar, D.G. Li, J.M. Shore, G.C.c 1992{BLOCKS IMPORT INNER MEMBRANE INSERTION MATRIX POLYPEPTIDE PORIN PRECURSOR PROTEINS TOPOGENESIS TRANSPORT UNCOUPLING PROTEINiNGA Signal-Anchor Sequence Selective for the Mitochondrial Outer MembraneOJournal of Cell BiologyN 119,6 1451-1457 DecQ,&Mcbride, H.M. Goping, I.S. Shore, G.C. 1996The human mitochondrial import receptor, hTom20p, prevents a cryptic matrix targeting sequence from gaining access to the protein translocation machinery- 1342307-3133Journal of Cell BiologyP,sodiumyhff6fye e e e de e eeeMeeeeFeeeee+eGeyeeeeeeXeeee e-ee&e.eeae e!^e!_e"2e$e&1e/e6e e=e e eeee#j#j#j0j6Cj6j6j8hj!jae!e!e VIbratiONal i  i* ia i i iz i i i" i%} i} i i ix i i) i4 iH iX i i1 i i q i  sA s sT s1 s s s8 s s  s  s  s  s!  s$ s&B s6& s  s i  i if i i4 iioe_ec!c"2ccQc ccc cc"2c#~c&c3NCbi3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3d3dE. Hunt, J.T. Porubcan, M.A. Wandler, C.F. Andersen, N.H. 19923-DIMENSIONAL STRUCTURE CLONING CONFORMATIONAL SEARCH CRAMBIN CYCLIC PENTAPEPTIDE ENDOTHELIN GEOMETRY INTERPROTON DISTANCE RESTRAINTS MOLECULAR-DYNAMICS NMR NUCLEAR MAGNETIC-RESONANCE PROTEIN CONFORMATIONS RECEPTORSolution Conformation of a Cyclic Pentapeptide Endothelin Antagonist - Comparison of Structures Obtained from Constrained Dynamics and Conformational Search FEBS Letters 2993o255-261 16 Mar1kM1l1o1r1s1~111111111111111111111111111111111/+/0++?22222/222222222closed the connection. Retrieving references 1 - 2... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 2... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Done retrieving references Done Connecting to host... Connecting to host... Searching for: [oh*[AUTH]+AND+murawski*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Retrieving r1Inmlc1"c1c1 c1,cXc0c1%c14c1;c1<c1Bc1Ic1Kc1Lc1Nc1Qc1Sc1Yc1^c1cc1dc1ec1rc1sc1yc1}c1~c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1c1ccc1c1c1c1c1c1c1c1c1c1c1ching for: [king*[AUTH]+AND+eisenberg*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 4 - 6... Sending message to server... Connecting to host... Client message sent The Host 1org1a1a1a1a1a1a1a1a1a1a1a1a1a1a2a2a2a2a2a2a/a2a2a2 a2.a/a/a24a2<a2Ba2Ea2Na2La2Ra2Ta2Xa2]a2aa2ba2da2ea2ga2ia2na2ra2sa2ta2va2~a2a2a2a2a2a2a2a2a2a2a2a2a2a2ac Rdiger, S. Peider-Mergener, J. Bukau, B.4b P                                   2rPOSTi2sa2ta2ua2va2wa2xa2ya2za2{a2|a2}a2~a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a2a1ja1Va2a2a2a2a2a2a2a2ang to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving reference number 4... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Done retrieving references Done Connecting to host... Connecting to host... Searching for: [spuy+vd*[AUTH]+AND+kana*[AUTH]]. Sending message to server... Client message sent Th490-496 Feb 2543LEGeorge, S.K. Xu, Y.H. Benson, L.A. Pratsch, L. Peters, R. Ihler, G.M. 1991BIOLOGICAL-MEMBRANES DIFFUSION ERYTHROCYTE-MEMBRANE MECHANISM MICROSOMAL-MEMBRANES MOBILITY PHOSPHATIDYLINOSITOL PHOSPHOLIPID-VESICLES RED TRANSLOCATIONCytochrome-b5 and a Recombinant Protein Containing the Cytochrome-b5 Hydrophobic Domain Spontaneously Associate with the Plasma Membranes of Cells$Biochimica et Biophysica Acta 10662131-143 22 Jul H  x1  7 33  2578LFGiannattasio, S. Marra, E. Abruzzese, M.F. Greco, M. Quagliariello, E. 1991JCMALATE-DEHYDROGENASE PRE-SEQUENCE PROTEINS TERMINAL SIGNAL SEQUENCEdThe Invitro-Synthesized Precursor and Mature Mitochondrial Aspartate Aminotransferase Share the Same Import Pathway in Isolated Mitochondria.'Archives of Biochemistry and Biophysicsr 290a2`528-534 1 NovZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=113990872VOGianni, S. Travaglini-Allocatelli, C. Cutruzzola, F. Bigotti, M. G. Brunori, M.rSnapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosae11399087 J Mol Biol 2001 309p5i1177-87. JAH81Gianni, S. Brunori, M. Travaglini-Allocatelli, C.C 2001aRefolding kinetics of cytochrome c551 reveals a mechanistic difference between urea and guanidine" @% Protein Sci108B1685-8.911468365 JAHhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11468365 http://www.proteinscience.org/cgi/content/full/10/8/1685 http://www.proteinscience.org/cgi/content/abstract/10/8/1685~wGianni, S. Guydosh, N. R. Khan, F. Caldas, R. D. Mayor, U. White, G. W. N. DeMarco, M. L. V. Daggett, V. Fersht, A. R.b 20036/Unifying features in protein-folding mechanismsProc Natl Acad Sci U S A 100o23 13286-13291 KSR 257981Gibbons, I.R. Asai, D.J. Tang, W.J. Gibbons, B.H.  1992CHLAMYDOMONAS FLAGELLA CILIA COMPLETE NUCLEOTIDE-SEQUENCE DYNEIN INNER-ARM DYNEIN ISOFORMS MESSENGER-RNA MICROTUBULE-ACTIVATED ATPASE MOLECULAR-CLONING MYOSIN PHENOL-CHLOROFORM EXTRACTION SACCHAROMYCES-CEREVISIAE SINGLE-STEP METHOD SPERM FLAGELLA<6A Cytoplasmic Dynein Heavy Chain in Sea Urchin EmbryosBiology of the CellB763303-309 2580$Gibbs, R.A. Mu, Y.Q. Wang, F.  1993ALCOHOLS BIOSYNTHESIS CLEAVAGE REACTION CYSTEINE ENANTIOMERIC PURITY FARNESYLTRANSFERASE IDENTIFICATION REAGENTS SYNTHASE TRANSFERASE\VThe syntheses of the deuterium-labeled farnesylated peptides 11 and 12 are described. The 500 MHz NMR spectra of these two compounds exhibit clear differences in the signals of the two pro-chiral hydrogens on C-1 of the farnesyl moiety. This provides a method to determine the stereochemical course of the enzyme farnesyl:protein transferase.PJAn NMR Method for Elucidating the Stereochemistry of Protein Farnesylation32s281-284 Feb0*Bioorganic and Medicinal Chemistry Letters@:Gibbs, A. C. Bjorndahl, T. C. Hodges, R. S. Wishart, D. S. 2002YProbing the structural determinants of type II' b-turn formation in peptides and proteins01.(Journal of the American Chemical Society 124S7t 1203-1213.11841288 JAHnZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11841288 2581*#Gibrat, J.F. Robson, B. Garnier, J. 1991piCODE RELATING SEQUENCE CONFORMATION GLOBULAR-PROTEINS INFORMATION PEPTIDES SECONDARY STRUCTURE PREDICTIONFInfluence of the Local Amino Acid Sequence upon the Zones of the Torsional Angles-phi and Angle-psi Adopted by Residues in Proteins  Biochemistry306r 1578-1586  12 Feb 2583"Gibson, K.D. Scheraga, H.A.  1991LEALANINE DIPEPTIDE AMBER CHARMM CONFORMATION ECEPP POTENTIALS PEPTIDESY2,Decisions in Force Field Development - Reply8t6 1109-1111 Junc4.Journal of Biomolecular Structure and Dynamics 2582<5Gibson, A.L. Wagner, L.M. Collins, F.S. Oxender, D.L. 1991ADENYLATE KINASE ATP HYDROLYSIS ESCHERICHIA-COLI GENE IDENTIFICATION MULTIDRUG RESISTANCE NUCLEOTIDE-BINDING FOLD PROTEINS SEQUENCE SITELIV-I, a high-affinity system that transports neutral, branched-chain amino acids into Escherichia coli, has two components, LivG and LivF, that are homologous to the cystic fibrosis (CF) transmembrane conductance regulator (CFTR). CF-associated mutations of human CFTR were introduced into corresponding regions of LivG, and their effects on leucine transport could be grouped into three classes. Mutations were found that (i) abolished LIV-I-directed transport, (ii) retained about a quarter of wild-type activity at the Michaelis-Menten constant (K(M)), and (iii) had minimal activity at the K(M). A mutation equivalent to a benign polymorphism had no effect on transport. The correlation of these mutational phenotypes in LivG and CFTR suggests that the LIV-I prokaryotic transporter is functionally similar to the CF protein and that this similarity can be exploited to clarify the properties of the nucleotide-binding fold in this superfamily of proteins.Fd^A Bacterial System for Investigating Transport Effects of Cystic Fibrosis Associated MutationsScience 254t 5028109-111 4 OctxAmmala)0ong iPHIpHILEs(! icityylaseoid-N (oosisg fNAlog's u(u"ues( yuysisd Hd tXtt3tttRt#t,tttstt]t*jt tical  n,qzed  ntharamaiah,chorNdtXffiff'fff>ff f nf f f f f Gf f f zf f Tf ffpff&fvffBff frfRRRRRRRRRRRRRRRZZZcccccckkkZZZRRRccckkkZZZRRRkkkZZZRRRZZZRRRZZZccccccZZZZZZccccccZZZZZZRRRZZZcccZZZRRRZZZcccZZZRRRZZZZZZZZZccccccccccccRRRRRRRRRccckkkZZZRRRRRRRRRRRRcccRRRRRRZZZcccZZZRRRZZZkkkkkkcccZZZZZZ1)!1)!1)!-afolding-grhr-nr-or,r-rr-sr-vrr-r-r-r}r$lrcr=r^rr-r-r-r-r-r-r-r-r-r-r-r-r-r-r-r,r-r-r-r-r-r-r-r-r-r.r. r.!r.,r.1r.6r.;r.BrrrrrrrrrrrrkDaeeegstra llisw<ndrewsselrTtnerhandke[idneyharat blmartinqmn%nnaseeSezeKeesee)e esinttic~s"s) sysr""r crtr'or-hg)g-ag!-dom rschnerlausner/ ingenberg nespelhownoehlhorni 6lstrupantinenrolev thakota)izlowskirappieg puijff#xSRo-u-u$ubotais}ntz$Jrodawsukawam#RwajimafL-a$K$a,Ta%ia%la%ka-a%a aa aa-4a-Ca-Fa-La,a-\a!a"a-da-ea-ua-ya-a-a-a a aaa-a-a-a-a-a-a-a-a-a-a-a-a-a-a-a-a-a-a.a.a. a.a#)a#(a#(a#(a#(a#(a#(a(#a(#a#(a#(aeional NMR spectroscopy: sequence-specific assignments, secondary structure, and dimer formation Biochemistry3020 4901-4909 21 May 5814Ota, M. Saito, N.4 1992AMINO-ACID SEQUENCE ANTAGONISTS DESIGN HYDROPHOBIC INTERACTION HYPERCALCEMIA INVITRO INVIVO ISLAND MODEL MALIGNANCY MECHANISM PARATHYROID-HORMONE-RELATED PROTEIN PEPTIDE SECONDARY STRUCTURE TERTIARY STRUCTURE TUMORvoPrediction of the Tertiary Structure of Parathyroid-Hormone-Related Protein ,zZ5O.5E,&Narayan, M. Welker, E. Scheraga, H. A. 2003HBCharacterizing the unstructured intermediates in oxidative folding Biochemistry42236947-55A Jun 1712795589 JAHPlehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12795589'jdBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301.,&Narayan, M. Welker, E. Scheraga, H. A. 2003Native conformational tendencies in unfolded polypeptides: development of a novel method to assess native conformational tendencies in the reduced forms of multiple disulfide-bonded proteins J Am Chem Soca 125a8  2036-7 Feb 2612590517 JAHilehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12590517}'piBaker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA. 5468Narayanan, P. Lala, K. 19923-DIMENSIONAL STRUCTURE AMINO-ACID SEQUENCE ANDROCTONUS AUSTRALIS HECTOR CENTRUROIDES-NOXIUS HOFFMANN LEIURUS QUINQUESTRIATUS QUINQUESTRIATUS NEUROTOXIN-I PEPTIDE VENOMHAPrediction of Tertiary Structures in Scorpion-Toxin Type ProteinsP Life SciencesP5010683-693O 54690)Narayanaswami, V. Kim, J.G. McNamee, M.G.P 1993{ALPHA-SUBUNIT AMINO-ACIDS BINDING ION CHANNEL LOCATION MEMBRANE PENETRATION DEPTH MODEL PARALLAX METHOD REGIONS THIOL-GROUPProtein-Lipid Interactions and Torpedo-californica Nicotinic Acetylcholine Receptor Function .1. Spatial Disposition of Cysteine Residues in the gamma-Subunit Analyzed by Fluorescence-Quenching and Energy-Transfer Measurements Biochemistry3246 12413-12419 23 Nov 5471*$Narberhaus, F. Giebeler, K. Bahl, H. 1992ACETOACETATE DECARBOXYLASE GENE BUTANOL CLONING VECTORS ESCHERICHIA-COLI EXPRESSION MYCOBACTERIUM-TUBERCULOSIS NUCLEOTIDE-SEQUENCE PROTEIN RNA TRANSCRIPTIONMolecular Characterization of the dnaK Gene Region of Clostridium-Acetobutylicum, Including grpE, dnaJ, and a New Heat Shock GenecJournal of Bacteriology2 174s10 3290-3299 Maye 5470Narberhaus, F. Bahl, H. 1992ANTIGEN BACTERIOPHAGE DNA ESCHERICHIA-COLI FREE-ENERGY PARAMETERS GENE GROWTH HEAT-SHOCK PROTEINS MYCOBACTERIUM-TUBERCULOSIS RNA DUPLEX STABILITYPd^Cloning, Sequencing, and Molecular Analysis of the groESL Operon of Clostridium-AcetobutylicumJournal of Bacteriologyi 17410 3282-3289A May& Nardi, F. Worth, G.A. Wade, R.C. 1997yLocal interactions of aromatic residues in short peptides in aqueous solution: a combined database and energetic alalysisFolding and Design2 S62-S68` JAH 5472leNarhi, L.O. Hua, Q.X. Arakawa, T. Fox, G.M. Tsai, L. Rosenfeld, R. Holst, P. Miller, J.A. Weiss, M.A. 1993ALPHA-LACTALBUMIN DETERMINANTS FACTOR-I LOCATION MOLECULE NMR NUCLEAR MAGNETIC-RESONANCE PANCREATIC TRYPSIN-INHIBITOR RECEPTOR SEQUENCEiRole of Native Disulfide Bonds in the Structure and Activity of Insulin-Like Growth Factor-1 - Genetic Models of Protein-Folding Intermediates Biochemistry3219 5214-5221 18 May 547482Narula, S.S. Dalvit, C. Appleby, C.A. Wright, P.E. 1988PJNMR studies of the conformations of leghemoglobins from soybean and; lupin& European Journal of Biochemistry 178e2419-435 15 Dec. 746 0 0 000y00000000*U0040300g000k0I000000 00 0*S0*T0)0+q0, 0,\0,0-f0- 0202!0006 0690H0m0$40 0,0/00)0.07~080700/0 <0 1t1t12 2_2 3_33k5$yE$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3$3%3%3%3%3%3%3%3%$3%/3%63%<3%E3%J3%S3%R3%T3%b3%3%3%3%3'W3%3%3%3%3%3%3%3%3&3&3& 3&3&3&3&+3&13&13&13&13#HEMOGLOBINS. HYDROGEN-ION CONCENTRATION. MALEATES. PROTEIN BINDING SUPPORT, U.S. GOV'T, P.H.S. THERMODYNAMICS. TROMETHAMINEJDA calorimetric study of the CO Bohr effect of monomeric haemoglobins& European Journal of Biochemistry623o577-582  1 Mar 2558Gerstein, M. Chothia, C. 1991hbAnalysis of protein loop closure. Two types of hinges produce one motion; in lactate dehydrogenase 2201P133-149' 5 JulH"Journal of Molecular Biology. Hoey19929Hofbauer199393 Hoff2001tj Hoffman1991  Hoffman1991  Hoffman1991: Hoffman1992 Hoffman1993= Hoffman1993  Hoffman1993/ Hoffman19987 Hoffman20002 Hoffman20017p Hoffman2002Hoffmann1991 Hoffmann1992 Hoffmann1992 Hoffmann19932Hoffmann2001D8RHoffmann2002r!' Hoffschulte1990! Hoffschulte1990!( Hoffschulte1992 Hoffschulte1994  Hoffschulte19946 Hoffschulte1997+\ Hoffschulte1998/9 Hoffschulte19997{ Hoffschulte1999f Hofhaus1989 Hoflack1993  Hofmann1990x Hofmann1991  Hofmann1991 Hofmann1992# Hofmann1993 Hofmann1995, Hofmann1998. Hofmann1998Q Hofnung1980 Hofnung1981 Hofnung1990h Hofnung1992X Hofnung199373 Hofnung1998 Hofrichter1992  Hofrichter1992  Hofrichter1993  Hofrichter1996 & Hofrichter1997 ) Hofrichter1997 ( Hofrichter1997 ) Hofrichter1997+ Hofrichter19987N Hofrichter1998- Hofrichter19995 Hofrichter20025? 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Hofmann1998Q Hofnung1980 Hofnung1981  Hofnung1990h Hofnung1992X Hofnung199337 Hofnung1998 Hofrichter1992  Hofrichter1992  Hofrichter1993  Hofrichter1996 & Hofrichter1997 ) Hofrichter1997 ( Hofrichter1997 ) Hofrichter1997+ Hofrichter1998N7 Hofrichter1998̧- Hofrichter1999Ė5 Hofrichter2002?5 Hofrichter2003O0 Hogan1987 Hogan1990 Hogberg-Raibaud1977  Hogervorst1991  Hogger1993 2 Hogness2000Hogquist19909  Hogue19935 Hogue20002 Hogue2002=1 Hohfeld2001E1 Hohfeld2001[1 Hohfeld2001`1 Hohfeld2001e1 Hohfeld2001T3 Hohfeld2001  Hohman1990  Hohn1979v Hohn1979v7 Hohsaka20007 Hohsaka20027 Hohsaka20027 Hohsaka20037 Hohsaka20037 Hohwy20027 Hohwy2002 Hoiby1991O Hoiby1993 Hoj1990 Hoj1991 Hoj1992 Hoj1992@6 Hoj1992 Hoj1993 Hoj1993 Hoj1993 Hoj19936 Hoj19936 Hoj1994 Hojo1991v Hojo1992. Hojo199996 Hojrup19969 Hol1992 Hol1992 Hol1993  Holak1988  Holak1988  Holak1989P Holak1990( Holak1991R Holak1992Q Holak1992& Holak1992J Holak1993 Holak1993> Holak1993 Holak19930 Holak2002 Holberton1993Holbrook1990 Holbrook1990hHolbrook1990Holbrook19918Holbrook1991Holbrook1992Holbrook19939Holbrook19939f Holbrook19939Holbrook1993h Holbrook19949 Holcomb1991 Holcomb1992/1Holdeman2000  Holden1987p" Holden19877  Holden1988 . Holden19922. Holden19931 Holden199391 Holford1999  Holifield1990  Holl1992v Holl19931 Holl-Neugebauer1991_ Holland1987"* Holland1989  Holland1991# Holland1991 Holland1992 Holland1993~& Holland1993  Hollecker1980  Hollecker1981  Hollecker1982  Hollecker1983* Hollenbach19977  Hollenbaugh1993  Hollenbeck1990  Hollenbeck1991 ! Hollenbeck1992  Hollenberg1991  Holler1992  Holley1990 t- Hollien1999L2 Hollien19991 Hollien2002 Hollingsworth1992 Hollinshead1991  Hollosi1990  Hollosi1990  Hollosi1991! 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Hollosi1993 Hollosi1993"Hollosi NOV 4 1992 Holloway1983:Holloway1991;Holloway1992a Holly1993  Holly1993  Holm1992v  Holm1992v  Holm1992v{ Holm1993e Holm19935 Holm19955Holmberg1991Holmberg1992  Holmes1983  Holmes19919 Holmes19919 Holmes1992 K& Holmes1993 + Holmes1993 Holmgren1984NiTta*u)u+u+ uZu"u%u u.u0"u+Cu2Eu4Qu5Mu*u4v6rvvaarkar,ierewa-xon.y2yaz"ogi!AJ'QJd K6K"wK1'K6%'K6r'K6'K8j'K$K1 3 3Ll7'l7'a8G'a*Sacee68+ m+ M/S/S/S/S/S/S/S/S/S/S/S/S/SHarper1993  Harper1993 ( Harrell1994  Harrington1990  Harrington1993  Harris19878  Harris1988 , Harris1990 Harris19919 Harris1992 " Harris1992 " Harris1992 " Harris1992 " Harris19929 Harris19921% Harris19939  Harris1993  Harris19939 Harris19933Harrison1982 Harrison1984 Harrison1985Harrison19888Harrison19899.NHarrison1< TRANSport7 ew e e ep e eQ e e e e e e% e)) e0 e0 e0 e)/ e+  e0 e6 e6N e6 e6 e6 e7$ e7= e7` e7a e7d e7f e7y e7 e7 e7 e7 e7 e8* e8A e8D e8v e edr r+h r& r+{ r6 r6 r7f r7y r7 r8` r< r s+ s, s  s  sK so s sp s s s s s A s  s, s sj s s s s  s s! s"_ sC s  s s6 s8F s s V g S$@ i6 i8i iC ip i6 i7 i  ing < s'P s  s6 S7= S%SABLE AmPHIpHILEs i icsV s o o  o  o x o oq o oJ oK om o o o o o o o  o o4 o  o!1 o!l o! o! o$ o% o'M o o oz i  i i iq iD i i& i i i i i! i" i# i* i7 i i i i i  i% i'O i'M i7 i8X i | ity/,y y+ PROceedings+ s+ s+ s, s+ s+ s+ s+ s, s) s) s& s) s, s, s," s,$ s,3 s,A s+ s,W s( s+ s,v s,w s,x s,y s, s, s, s, s, s, s, s& s, s, s- s s, s-, s, s+; sM s{ s s[ s% s sw s  s  s s sN s-1 s-2 s-3 s-4 s-4 s-4 s4- s h`XPxPH@80( H0GP`XH@80(8 GxphG80(LChasingArrowsLPeriodicalILBroadcasterILAttachableILPaneJ(J JLControlI(JfJ J(J4LControlPaneI(JjJ tein folding: evidence from the lattice model Biochemistry33 10026-10036$ JAH124-Abney, J.R. Scalettar, B.A. Hackenbrock, C.R.i 1990AGGREGATION CLUSTERS DEPENDENCE INTERACTING MEMBRANE-PROTEINS LATERAL INTERACTIONS LIGHT-SCATTERING MODEL MOLECULES MUTUAL DIFFUSION SELF-DIFFUSIONExqOn the Measurement of Particle Number and Mobility in Nonideal Solutions by Fluorescence Correlation SpectroscopyyBiophysical Journal 581o261-265` Jula+)_^\.][Z>YXWRTUjEmr, S.D. Silhavy, T.J. 1982(!The signal hypothesis in bacteria2,Progress In Clinical and Biological Research91(Membr. Growth Dev.) 3-14 1999A review and discussion, with 27 refs., on the function of the extra peptide, the signal sequence, of the amino termini of secreted proteins of bacteria. 0361-7742 1998Emr, S.D. Silhavy, T.J. 1982The mechanism by which the LamB protein is exported to the outer membrane of Escherichia coli was studied. By 2 selection procedures based on gene fusions, a no. of mutations that cause alterations in the LamB signal sequence were identified. Although many such mutations block LamB export to >95%, others have essentially no effect. This enables an anal. of the functions performed by the various mol. components of the signal sequence. Apparently, a crit. subset of 4 amino acids is contained within the central hydrophobic core of the LamB signal sequence. If this core can assume an .alpha.-helical conformation, these 4 amino acids comprise a recognition site that interacts with a component of the cellular export machinery. Since mechanisms of protein localization appear to have been conserved during evolution, the principles established by these results should be applicable to similar studies in eukaryotic cells. 0021-9525953l689-696pd]Molecular components of the signal sequence that function in the initiation of protein exportJournal of Cell BiologyEmr, S.D. Silhavy, T.J. 1983VOImportance of secondary structure in the signal sequence for protein secretion.08015 4599-4603d 2000B;Mutant Escherichia coli strains in which export of the LamB protein (coded for by the lamB gene) to the outer membrane of the cell is prevented were described previously. One of these mutant strains contains a small (12-base pair) deletion mutation within the region of the lamB gene that codes for the N-terminal signal sequence. In this mutant strain, export but not synthesis of the LamB protein is blocked. Pseudorevertants were isolated that restore export of functional LamB protein to the outer membrane. DNA sequence anal. showed that 2 of the revertants contain a point mutation in addn. to the original deletion. These point mutations lead to amino acid substitutions within the signal sequence. These secondary mutations efficiently suppress the export defect caused by the deletion mutation. Anal. of the secondary structure of the wild-type, mutant, and pseudorevertant LamB signal sequences suggests that the secondary mutations restore export by allowing the formation of a stable .alpha.-helical conformation in the central, hydrophobic region of the signal sequence. 0027-8424VOProceedings of the National Academy of Sciences of the United States of Americag 2001 Emsley, L. Bodenhausen, G. 1991CLASSIFICATION COHERENCE CONNECTED TRANSITIONS CYCLOSPORIN-A EVOLUTION PERIOD PSEUDO-COSY PULSES RESOLUTION SPECTRA TWO-DIMENSIONAL SPECTROSCOPYjdSelective 2-Dimensional NMR Experiments for Topological Filtration of Fragments of Coupling Networks.(Journal of the American Chemical Society 1139q 3309-3316m 24 Apr 2002"Emtage, J.L.T. Jensen, R.E.  1993ADP-ATP CARRIER CONTACT SITES CYTOSOLIC DIHYDROFOLATE-REDUCTASE EXONUCLEASE-III INTERMEMBRANE SPACE NUCLEOSIDE TRIPHOSPHATES OUTER-MEMBRANE PRECURSOR PROTEINS PROCESSING PROTEASE SACCHAROMYCES-CEREVISIAE jdMAS6 Encodes an Essential Inner Membrane Component of the Yeast Mitochondrial Protein Import PathwayJournal of Cell Biology 1225t 1003-1012t Sep 200381Encinas, M.V. Rojas, M.C. Goldie, H. Cardemil, E.c 1993BINDING-SITE CHICKEN CONFORMATIONAL CHANGE GENE INDOLE MESSENGER-RNA MITOCHONDRIAL PHOSPHOENOLPYRUVATE CARBOXYKINASE NUCLEOTIDE BINDING NUCLEOTIDE-SEQUENCE PHOSPHO-ENOL PYRUVATE CARBOXYKINASE PROTEIN RESIDUES TRYPTOPHAN FLUORESCENCEComparative Steady-State Fluorescence Studies of Cytosolic Rat Liver (GTP), Saccharomyces-Cerevisiae (ATP) and Escherichia-Coli (ATP) Phospho Enol Pyruvate Carboxykinases$Biochimica et Biophysica Acta1 1162 1-21195-202- 5 Mar,&Endo, T. Ueda, T. Yamada, H. Imoto, T. 1987~wpH dependence of individual tryptophan N-1 hydrogen exchange rates in lysozyme and its chemically modified derivatives.r Biochemistry26 1838-1845 JAH 2005Endo, T. 199182Protein folding and transport in cells. [Japanese]362p128-136 Feb@:Tanpakushitsu Kakusan Koso (Protein, Nucleic Acid, Enzyme) 2004Endo, T. 1991VPATP CATALYSTS HSP60 HSP70 MITOCHONDRION MOLECULAR CHAPERONE PROTEIN IMPORT STATExqCo-operative Binding of hsp60 May Promote Transfer hsp70 and Correct Folding of Imported Proteins in MitochondriaO FEBS Letters 293K 1-2 1-3U 18 Nov 2006&Endo, T. Kawamura, K. Nakai, M.m 1992~xANALOGS BINDING CARBOXYLASE ENVELOPE FOREIGN PROTEIN IMPORT MEMBRANE MITOCHONDRIAL PRECURSOR PROTEIN SEQUENCES TRANSPORTThe Chloroplast-Targeting Domain of Plastocyanin Transit Peptide Can Form a Helical Structure But Does Not Have a High Affinity for Lipid Bilayers& European Journal of Biochemistry 2072e671-675 15 Jul 2007Endow, S.A. Titus, M.A. 1992ACTIN BINDING SITES BETA-TUBULIN GENE CAENORHABDITIS-ELEGANS COAT-COLOR PHENOTYPE DYNEIN DYNEIN-LIKE PROTEIN GENETIC INTERACTIONS KINESIN KINESIN-LIKE PROTEIN MATERNAL MESSENGER-RNA MOTOR PROTEIN MUTANTS MYOSIN MYOSIN HEAVY-CHAIN SQUID GIANT-AXON TRANSLOCATES MICROTUBULES INVITRO,&Genetic Approaches to Molecular Motors|vAnnual Review of Cell Biology 8; 29-66; Annual Reviews Inc, 4139 El Camino Way, PO Box 10139, Palo Alto, CA 94303-0897(!Enenkel, C. Blobel, G. Rexach, M. 1995zsIdentification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes&Journal of Biological Chemistry 27028 16499-16502.'Enenkel, C. Lehmann, A. Kloetzel, P.-M.` 1998Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast EMBO Journal1721 6144-6154 2010.'Engel, M. Williams, R.W. Erickson, B.W. 1991CELL-ADHESION INTEGRINS MODEL PROTEIN QUATERNARY STRUCTURE RAMAN AMIDE-I RECEPTORS SECONDARY STRUCTURE SOLID-PHASE SYNTHESIS STABILIZATION TROPOMYOSINhaDesigned Coiled-Coil Proteins - Synthesis and Spectroscopy of Two 78-Residue alpha-Helical Dimerst Biochemistry3013 3161-31690 2 Apr0Suchn0a0a0aza52a5a6a6a6a6a6a6a6"a6#a6%a6&a6'a6(a64a65a6Ba6La6Ma6Pa6Ra6`a6ua6za6{a6}a6a6a6a6a6a6a6a6a7a7a7*a7:a7;a7<a7Ca7Da7Ha7Ka7La7Pa7ca7wa7xa7a7a7a7a7a7a7a7a7ah"h3hhhskimr mpanostomy)pec*Rhh"h3hhhen @ |82U8418918:18<18?18@18A18B18C18D18E18H18I18J18K18N18O18P18Q18S18T11"1)1)16161111 1 1$1)1)-1+p16x16161617/171717187=Wev7Aa7Ca7Ea7Fa7Ga7Ia7Ka7Xa7]a7^a7_a7`a7aa7ba7da7ea7fa7ia7ja7la7na7oa7pa7qa7ra7ta7ua7va7wa7ya7}a7~a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7ato and across the membrane or enhancing the protease resistance of these domains. We now show that some SecA bound at SecYEG is accessible from the periplasm to a membrane-impermeant probe in cells with a permeabilized outer membrane but an intact plasma membrane.'d]Department of Biochemistry, Dartmouth Medical School, Hanover, New Hampshire 03755-3844, USA.tEichler, J. Wickner, W.("99009017 0021-9193 Journal Article J Bacteriolab[Adenosinetriphosphatase/*metabolism Bacterial Pr4#N4*a4Da4?a4Aa4Ia4Xa4ba4_a49a4a4ya4}a4a4a4a4a4a4aa4a4a4aUaaaa&a%Da59a5Va5da5ca5fa5qa5ya5xa5ta5a5a5a5a5a5a5a5a5a5a5a5a6a6a6 a6a6a6a6a6a6a6 a6:a6@a6Ga6SaF BRAIN TUBULIN CO-SOLUTE INDUCED STABILIZATION OF PROTEINS CRYOPROTECTANT DIVALENT-CATIONS ENHANCED PROTECTION FREEZE-DRIED LIPOSOMES FREEZE-INDUCED DENATURATION INCREASED THERMAL-STABILITY LYOPHILIZATION-INDUCED DENATURATION POLY(ETHYLENE GLYCOLS) PREFERENTIAL INTERACTIONS PROTEIN STABILIZATION PROTEIN-DEGRADATION RIBONUCLEASE-A SOLVENT DENATURATIONlHBFactors Affecting Short-Term and Long-Term Stabilities of Proteins$Advanced Drug Delivery Reviews101s 1-28Jan-AprL6d)$# )">#^+[+^e//)F1?1a1u1y111122Y2a2g2223/343L3]3U33334+4&4R4d5L5N5d5_5x5555666 6 6W6Y6q6666SSSS$ SSSSS0S_SSSSSSSSS"S&{S6ES-S@SS aaa+`a71a7a Vase)S 9 IFICATION E/EE+xEEDs 'sZii iiii i !s s s8sBs@s'Qs svvez&=y imate Gd6sdd0CoLiV+ czc0c0c4)c5c5c5c6c63c6=c6@c6Dc6Gc6Kc6Oc6fc6yc6c6c6c6c6c6c6c6c6c6c6c6c6c6c6c6c6c7c7c7"c7#c7&c7'c7,c7.c73c75c76c7:c7>c7Cc7Ic7Xc7ac7ec7gc7rc7uc7wc7yc7{c7|c7}c7cmatically reduced the solubility of the same fusion proteins. The mutations with the most profound effect on solubility were shown to reduce the global stability of MBP.:'Protein Engineering Section, Macromolecular Crystallography Laboratory, National Cancer Institute at Frederick, Frederick, MD 21702-1201, USA.,%Fox, J. D. Kapust, R. B. Waugh, D. S.eng Journal Articlen*ATP-Binding Cassette Transporters *Amino Acid Substitution/genetics Bacterial Proteins/chemistry/genetics Carrier Prondence of protein stability#"Journal of Molecular Biology 294t 1051-1062[ SJE 1960LFElias, D. Reshef, T. Birk, O.S. Vanderzee, R. Walker, M.D. Cohen, I.R. 1991LEADJUVANT ARTHRITIS ENCEPHALOMYELITIS EAE LINE CELLS MELLITUS NOD MICETpjVaccination Against Autoimmune Mouse Diabetes with a T-Cell Epitope of the Human 65-kDa Heat Shock Protein888 3088-3091 Apr1VOProceedings of the National Academy of Sciences of the United States of AmericamStates'^sssssrsssss6ssssVssss4sbsdscs<sUsbssssjsssss(skssssss!s6s*|sssss s s s s s s s s s s s s s s s sARYCircular Dichroism and Fourier-Transform Infrared Spectroscopic Studies on T-Cell Epitopic Peptide Fragments of Influenza Virus HemagglutininI:3Biochemical and Biophysical Research Communications  1933S 1247-1254E 30 Jun 3262Holm, L. Sander, C. 1992hbDATABASE DESIGN PREDICTION PROTEIN FOLDING PROTEIN-STRUCTURE ROTAMERS SEQUENCE SIMULATED ANNEALINGyFast and Simple Monte-Carlo Algorithm for Side Chain Optimization in Proteins - Application to Mod bPerutzc cs s s bSv#vLvMvPvOvNvRvQvVvUvTvSvXvWvYv^v]v\v[vZv`v_vbvavdvcvevpvvvvushinSf S+ S+ S. S. S- S. S. S3 S9 S +Senson9istence old Gs Ks Js#sFsingn8 n n #ticide_tach8jasLS Uerhs(a(a52a8`'aianderlk,kofsky+<mans J.W. 1998\VInhibiting transthyretin conformational changes that lead to amyloid fibril formation.VOProceedings of the National Academy of Sciences of the United States of America95 12956-12960 SJE Px1998amyloidCchangesconformationalfibril formationH InhibitingJKelly KlabundeLashuellead PetersonPurkeTABita!l#l3(less$sws"Bcuwu"Buuchis7latedshichiasbbbbanay y!? y!@ y/ y1 y4b y ykininr  rL p%0 Splesinuuslrolimus6 d8< d8p d8 dRdak!k4Qk!Akid+dei,+o+o-ro.o/_o0o0o3o6o7o8?oo esse e'Oejon'7z'u7'uuschf/f/g1Ug1\g1_g1`g1kg2g2g2g2g20g%g&Ga1a7a8a+a7a7Ca7a8a8a88a8<akashiray y 8yag)8g)9g)7g!Bg2gart0+Med6i0i7&ibing liavini!C uuchieeeeeation of Pore Size and Pore Line Tension$Biochimica et Biophysica Actao 11471 2>NCbi2?d2Bd2@d2Cd2Dd2Ed2Id2Hd2Gd2Fd2Jd2Kd2Nd2Md2Ld2Pd2Qd2Rd2Td2Sd2Vd/d2Xd2Zd2Yd2[d2\d2]d2_d2^d2`d2ad2bd2dd2cd2ed2fd2gd2id2hd2jd2nd2md2od2pd2qd2rd2sd2td2ud2vd2wd2xd2yd2zd2{d2|d2}d2}d2}d2}d2}dts. 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Disclaimer THE NLM DATABASES ARE INTENDED FOR INFORMATION1'ofi1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a1'a2s'a2t'a2u'a2v'a2w'a2x'a2z'a2{'a2|'a2~'a2'a2'a2'a2'a2'a2'a2'a2'a2'a2'agAGards s $o o o o oooQo`o-oo|o~o}o$o$o$o+o-o.Ro0 o1o ose+ss1Draberes,she"w+Dw1w2w#wab2b$backjjxjeee)Hi$i0?iiii&dCdiCi(i!Diingntk%~s-s sssOsLscell$*1711w1M11x1111111111111111Q1j111'111$1%1o111 1111 1 1!'1!f1"M1#1%1%&1%'1&01)'1+\111+w1+1+1+1+1,10152151516 1616"16+16-16316?16j16161616161616161717171717!17#17&17717917:17H17a17g17j17{17171717171717171717171717171717181818P18Q18`18b18h181818181p1+h1+j1+j1=m&form=6&dopt=r2&dopte2+r2-r2.r21r22r23r24r25r26r27r28r29r2:r2;r2<r2=r2>r2?r2Br2@r2Cr2Dr2Er2Ir2Hr2Gr2Fr2Jr2Kr2Nr2Mr2Lr2Pr2Qr2Rr2Tr2Sr2Vr2Xr2Zr2Yr2[r2\r2]r2_r2^r2`r2ar2br2dr2cr2er2fr2gr2ir2hr2jr2jr2jr2jr2jr2jr message to server... Client message sent The Host closed the connection. Retrieving reference number 1... 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Client mes -Addition :aEa2aa$aXaZa`aaa^a]aaaaa+ aMaOaaaa aaaaaa)a)aa!a"a)a#{a#a#a%a)a+Za+_a-a+sa#a0a0a5a5a5a5a6 a6a6"a6:a6_a6ga6pa6a6a6a6a6a1526#7H71N'01g'71'71'71'71'76p'7177I33'919 s8 9T9!9J9.>9 9\3&;1016-161K1 11 17,9.>3,38i88.808 f8 8 8898;88 58)8"8#8#98#8-8u8182P838484e84_85S8!8c8c87qPUBMed7rC7sC7tC7uC7vC7wC7xC7yC7zC7{C7|C7}C7~C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C7C Unintegratedw-rruptedqueTTT&t 7t 6t=ttt'tt t"t%t.t/t6 t6Gtt&t&'tztt Yt -n jn n)n+ nnnnMn,n)n!n"n+n+{n+n0n5l5l5l6l6+l6Gl6_l6fl6{l6l6l6l6l7)l7il7kl7ol8Y20038Z38[38]38_38`38a38b3838383838383838383838383838383838383838383838383838383838383838383838383838383838383838383839393939393939#39'39(39*39839K39&38353739^393835838!36L38383Z3)*32'345'37w1641383838383838383838383838383838383838383838383838383838383838383835838!36L38383Z3)*32'345'37w1641RLCrystal structure of ovalbumin as a model for the reactive centre of serpins Nature 347U 6288 99-102 6 SepU 7496Stein, P. Chothia, C. 1991ALPHA 1 ANTITRYPSIN ANTITHROMBIN CONFORMATIONAL CHANGE CRYSTAL-STRUCTURE HUMAN ALPHA-1-PROTEINASE INHIBITOR LIMITED PROTEOLYSIS OVALBUMIN PACKING PLAKALBUMIN PROTEIN STRUCTURES SERPIN STRUCTURE.(Serpin Tertiary Structure Transformation 2212615-621y 20 Sep"Journal of Molecular Biology5Gov5'/'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'5'However?llllllllllll)$lvl)llllll~l ll l!l!ol!nl"yl#^l#zl#l#l)l%'l%l)&l),l)1l+\l+jl&l+yl+~llNl).l+l0l0l0l0l0l0l0l5l6 l6l6l6l60l61l63l.$kProceedsn6s as ss)s s7%s8}ssseee?ee0ee se e !e ee/ee.eee$eee''eye9e~e)7e"e#e$e%-e+e-Ne.De.e/e/e/ee0e2e3e,e5Ye5be7 e7)e99eee8eeeeheqe/eeteSe Ye Ye YeState s s s qs s&s s s6sssssXsZsjss&sssssssRsesss_s~s Ns Zs!os!ns!s"Ms# s#qs#s%s+_s+`s+js'Qs-s#s0s0s0s=s4s5s5s5s6s6s6s6s6s6s6)s6)sEXCHANGEwllkl~lll ll.lllll<l>lll%lHlllqlwlllllllcllGl!llll bl l l l!l"l#l#l#l#l#l%=l%Il%_l%al%l%l%l&Pl&slrl]l\llnlpl172 9  5030-5034L Sep0 3111,&Hellinga, H.W. Wynn, R. Richards, F.M. 1992BURIED ASPARTIC-ACID CONFORMATIONAL TRANSITIONS DENATURED THIOREDOXIN GENETIC-ANALYSIS GLOBAL STABILITY GUANIDINE-HYDROCHLORIDE LAMBDA-REPRESSOR MUTANT THIOREDOXINS PROTEIN STABILITY STAPHYLOCOCCAL NUCLEASE~The Hydrophobic Core of Escherichia-Coli Thioredoxin Shows a High Tolerance to Nonconservative Single Amino Acid Substitutions Biochemistry3145 11203-112095 17 Nov-S-c-c-c-c-Oc>c-c-c-c-c-c-c-c-c-c-c-c.c. c.c.c.c.c.c. c.!c.0c.;c.Bc.Lc-c.Ac-c.Ec.Oc.Uc.[c.\c.]c./c.bc-Qc.lc.mc.uc.rc.pc.vc.zc.c-c-c-c-c-c-c-c-c-c-c-c-c-c#0Peptide#6s#Vs#s#s#s#s#s#s#s$s$s$ s$Is$Js$s$s$s$s%s%s%&s%)s%/s%as%}s%s%s%s%s%s%s%s%s%s&s&+s&Cs&Bs&>s&Js&s&zs&s)%s)&s+Zss+_s+`s+as)sssss+s+s+s+s+s+s+sN АA L| N ؐA L| N  A L| N ̐A L| N A L| N 8A L| N A L| N lA L| N pA L| N A L| N A L| N PA L| N ĐA L| N A L| N A L| N A L| N (A L| N XA L| N A L| N A L| N lA L| N !^Chemical!]s!hs!js!{s"s" s"%s"s"s"s"s"s"s#Hs#s#s$s%s%s%s%_s%s'Ws%s%s%s&,s&as&hs&s&s'&s)sss+s+s+s+s+s+s+s+s+s+Bss s+s,s-s-$s-&ss,s+s#s ssssss F. Hartmann, E. Gorlich, D. Rapoport, T.A.c 1990DOCKING PROTEIN IDENTIFICATION IMMUNOCYTOCHEMISTRY MICROSOMAL-MEMBRANES POLYPEPTIDE PREPROLACTIN QUANTITATION RAT-LIVER RECOGNITION PARTICLE RECEPTOR TRANSLOCATIONf_Segregation of the Signal Sequence Receptor Protein in the Rough Endoplasmic Reticulum Membrane& European Journal of Cell Biology532197-202 Decy 82014-Vogel, S.S. Chernomordik, L.V. Zimmerberg, J.t 1992ztCELL INFLUENZA-VIRUS LIP\disTincttl l Ol fl l llll*llTlnl)Yll3ll2lllhll'l l,llll<l;ll!7l"Vl"dl)Ol*8l$l$l%l%l&%l&.l+[l+rl,l-|l.Nl.l-pll/l0 l0Ol0l1@l1rl2l2l4l4Ll6llllllllallTl l"l xyLy]yldatedIFdamsoditionallyE eNINEIyly ylimidodiphosphateJhesions}JuvantspPRenalsorptionvanceseY`ing<DVATEdCing on eorei itiesQ9Y0000~0}0*00000 a0 m0 |0 0 0 r0 0 0 0 0 0 10 X0 0 0 b0 0 80 0' 0 0 00000P000Q0y000;0h000*000000000e000000* 1997'`8(8, 8)8)8,8+F8+8(8* 8,#8,*8+8,-8,68,78(8*8&8*8* 8*8,H8,Q8,V8,Z8,]8,^8,d8,e8(8&8,f8,h8,o8,p8(8&8(8&8,u8,v8,w8,|8*w8,8,8,8,8,8,8,8,8&8,8,8,8,8,8,8,8,8tional Changes of the alpha(1)-Proteinase Inhibitor Affecting Its Cholesterol Binding Ability FEBS Letters 3233n236-238 1 Jun 3528 Janecek, S. 1993(BETA-ALPHA)8 BARREL ALPHA-AMYLASE AMINO-ACID SEQUENCE BACILLUS-SUBTILIS GENE HYDROPHOBICITY NUCLEOTIDE-SEQUENCE PROTEIN STABILITY SUBTILIS ALPHA-AMYLASE THERMOSTABILITYDoes the Increased Hydrophobicity of the Interior and Hydrophilicity of the Exterior of an Enzyme Structure Reflect Its Increased Ther,y Structure, s, s,} s, s, s9 s, s, s, s* s+ s-  s- s- s9 s* s s s s s? s  s+ s% s% s-( s-) s-* s s& s s& s  s s s s sA sn sq sM s s  s s2 s s s) s  s{ s$G s$ s%i s%k s s s s s s s s scZcZZRcZcZZRZRQRRJJBBB9191911) () 91B9B999 1) () () wZG9)1.YaPwɪ۽ưڽֺơưɲֺʰֺʰɲ_IB) ) ! ! ! ! ) B9WI.ươֺֺơ˽ư˺ưαươYaP9191B9J9JBRJRJJ9B9JBJBB9B9J9B9B1B9J9RBZJRJZJZJZJZJZJZRcZcZZJJBJ9RBJBJBRBRJRJRJRJRJZJZJRJRJRJJBJB  " 2 ,   $ 3P++   8>7Gross, C. Koelch, W. DeMaio, A. Arispe, N. Multhoff, G.` 2003|Cell-surface heat shock protein (Hsp70) mediates perforin-independent apoptosis by specific binding and uptake of granzyme B J Biol Chem 278y 41173-41181 2843:4Grosse, F. Krauss, G. Knill-Jones, J.W. Fersht, A.R. 1984xqReplication of phi X174 DNA by calf thymus DNA polymerase-alpha: measurement of error rates at the amber-16 codon 179535-5404-Advances in Experimental Medicine and BiologyB i2 i#b i s)s)1i*ientd#d%d -d+dde e e e eeeeeYi-iqiMe+ediQiqi'2ing'> i2 i i*ientd -dde e e e eeeee"HEa2+a2.aa21a/a2Na2ba0~a2ta2ua2wa2|a2a2a2a2a2a2a2a2a2a2a2a2a2a/!a2a2a2a2a2a2a2a2a2aea2a2a2a2a3 a3a3a3a3a33a3:a3>a3Ba3Ca3Da3Ga3Ia3Na3Ra2a3da3]a3\a3\a3\a3\a) * + , - . / 0 1 2 3 4 5 6 7 8 9 : ; < = > ? @ A B C D E F G H I J K L M N O P Q R > Levinthal, t t2 t' t* t+ t. t"tan t rrrDrErGr r@zz z!z"z3zz!z&z-#zFz48z4z8z8z zkirat<ylw$w#w*lwwww#Gw w+w6%w6`w6rw9+ww%iii"i"Fi#Di#Fi#Eiickiss1Fwy Sh h hhh&h'h!>`@!>a^0 !>[!>`pp!>a@!0d!0p F!>`p*x!00 !>`0!>a@!0!0H!>`p!>`p!>a!0!>`p!>ap!>a!>`pt!0!>a@@!>a^0 !>`p!>ap !>a '!>`p!>Z@!>b !>Z@!>a`!>b,D!>Z@DFF!>a- 1998.9.9.9.9-9.9-9*9/9)9.9+39)9+9+t9+Y9/9/9,9)90909*90?90V90X90Z9)90]90e909090909090909090909090909091 90`9*909+ 91919191~91919191919191919+9 m  n  o  p  q  r  s  t  u  v  w  x  y  z  {  |  }  ~                           0} Molecular0 E0 E0 E0 E0 E0 E0 E0 E0 E0 E0 E0 E0 E# E# E0a E/9 E)0 E. E1 E0 E, E0 E1. E# E1 E0 E1 E1 E1 E1 E E1 E1 E1 E+ E. E E E, E/ E+C E* E/ E/ E0 E2 E, E3 E3 E3 E3 E3A E3B E3C E3D E3E E3F E3G E3H E3I E3J Ez c-%$!? /!;!a % ā$=%$䫦礐ﭯ޿O巕 $}絷!!䧧#1!5$0彅 Ō!$!巀%- %ߤ턽%c> 4`a秽ww7!'$q$- %$!)㯵$!  '$$4 t!1EAIN MINIFILAMENTS PHOSPHORYLATION SEQUENCEIdentification of Functional Regions on the Tail of Acanthamoeba Myosin-II Using Recombinant Fusion Proteins .2. Assembly Properties of Tails with NH2-Terminal and COOH-Terminal DeletionsNJournal of Cell Biologyn 1116n 2417-2426n Dec0*Sinclair, J.F. Ziegler, M.M. Baldwin, T.O. 1994PJKinetic partitioning during protein folding yields multiple native states.15320-326h Nature Structural Biology7 \'&`2'%4'$'#'"'!./'' ''x'R'' 8870 Zwieb, C. 1991B;19-KDA BINDING COMPONENT DOMAIN MEMBRANE SITE TRANSLOCATIONf`Interaction of Protein SRP19 with Signal Recognition Particle RNA Lacking Individual RNA-HelicesNucleic Acids Research1911 2955-2960 11 Jun 8871 Zwieb, C.0 199119-KDA DOMAIN ENDOPLASMIC-RETICULUM MEMBRANE MESSENGER-RNA PROTEIN RNA BINDING SEQUENCE SIGNAL RECOGNITION PARTICLE SITE-DIRECTED MUTAGENESIS TRANSLOCATIONA Basic Region Neighboring the Lysine-Rich C-Terminus of Protein SRP19 Is Required for Binding to Signal Recognition Particle RNAJ699649-654 Sep9$Biochemistry and Cell Biology 8872 Zwieb, C. 1992vp4.5 S-RNA 7SL RNA BINDING CENTRAL DOMAIN COMPONENT ESCHERICHIA-COLI RIBOSOMAL-RNA SEQUENCE SRP RNA TRANSLOCATION`YRecognition of a Tetranucleotide Loop of Signal Recognition Particle RNA by Protein-SRP19e&Journal of Biological ChemistryP 267 22 15650-15656 5 Aug 8873 Zwieb, C.p 19927SL RNA CENTRAL DOMAIN CHLOROPLAST GENOME COLI RIBOSOMAL PROTEIN-S15 ESCHERICHIA-COLI GENE ORGANIZATION MODEL NUCLEOTIDE-SEQUENCE SECONDARY STRUCTURE SIGNAL RECOGNITION PARTICLEgRKConformity of RNAs That Interact with Tetranucleotide Loop Binding ProteinsrNucleic Acids Research2017 4397-4400 11 Sep 8874Zwieb, C. Larsen, N. 1992SEQUENCE4.The Signal Recognition Particle (SRP) DatabaseNucleic Acids Research20 2207 11 May2+Christian Zwieb Florian Muller Niels Larsen 1996\VComparative analysis of tertiary structure elements in signal recognition particle RNAFolding and Design147315-324 JLFZwieb, C Samuelsson, T 199960The Signal Recognition Particle Database (SRPDB)Nucleic Acids Research271 169d 8875^XZydowsky, L.D. Etzkorn, F.A. Chang, H.Y. Ferguson, S.B. Stolz, L.A. Ho, S.I. Walsh, C.T. 1992CALCINEURIN CATALYSIS CIS-TRANS ISOMERASE CONFORMATION CYCLOPHILIN CYCLOSPORIN-A ESCHERICHIA-COLI FKBP-FK506 IMMUNOSUPPRESSANT FK506 IMMUNOSUPPRESSION MUTAGENESIS PEPTIDYL-PROLYL ISOMERASE PROTEIN SENSITIVITY T-CELL ACTIVATIONActive Site Mutants of Human Cyclophilin-A Separate Peptidyl-Prolyl Isomerase Activity from Cyclosporin-A Binding and Calcineurin InhibitionProtein Science219  1092-1099h Sepp 8876BS-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-S-SRszRsz:ckV{cV{cV{p١xPM@peTdR2T"ԹАm{bIeTАmXkk931931;BEWZZfkkkss{9. B 9. dR2g]RWZZMQTMQTBPO98;;BE;BE;BE;BE;BEMQTԹ׽١xԹ辤辤١x辤eT|ףԹp١xΔףdR2MQTWZZMQT;BE98;BPO;BEMQTMQT98; %fkk9JIZcc{9JIPcc';BEMZcg]RlQ, 931OB29( MQT9319JRVn0 5083 1990AQUEOUS-SOLUTION COHERENCE-TRANSFER CORRELATED SPECTROSCOPY PROTEIN CONFORMATIONS PROTON PROTON DISTANCES RABBIT-LIVER METALLOTHIONEIN-2 RAT-LIVER SECONDARY STRUCTURE SPIN SYSTEMS TWO-DIMENSIONAL H-1-NMRe3-Dimensional Structure of Human <(CD7)-CD-113>Metallothionein-2 in Solution Determined by Nuclear Magnetic Resonance Spectroscopy 2143 765-779 5 Aug"Journal of Molecular BiologyF?Messerle, B.A. Schaffer, A. Vasak, M. Kagi, J.H.R. Wthrich, K.y 5082 1990rlBINDING COSY IDENTIFICATION PROTEINS RABBIT-LIVER METALLOTHIONEIN-2 RAT-LIVER RESOLUTION SECONDARY STRUCTUREjdAmide Proton Exchange in Human Metallothionein-2 Measured by Nuclear Magnetic Resonance Spectroscopy 214 3781-786 5 Aug "Journal of Molecular BiologyNGMesserle, B.A. Bos, M. Schaffer, A. Vasak, M. Kagi, J.H.R. Wthrich, K.y 5085,%Mesters, J.R. Degraaf, J.M. Kraal, B. 1993ACTIVATION ALUMINUM ION FLUORIDE FUSIDIC ACID G-PROTEIN G-PROTEINS GAMMA-PHOSPHATE GAMMA-PHOSPHATE ANALOGUE GTPASE EFFECTOR GUANINE-NUCLEOTIDE BINDING CENTRE HYDROLYSIS INHIBITION MECHANISM TRANSLATIONAL INHIBITION TRANSLOCATIONDivergent Effects of Fluoroaluminates on the Peptide Chain Elongation Factors EF-Tu and EF-G as Members of the GTPase SuperfamilyA FEBS Letters 321m 2-3149-152 26 Apr 5086NGMetzger, J.W. Sawyer, W.H. Wille, B. Biesert, L. Bessler, W.G. Jung, G. 1993BACTERIAL LIPOPROTEIN BINDING-PROTEINS EPR ESCHERICHIA-COLI LIPOPROTEIN FLUORESCENCE FLUORESCENCE MICROSCOPY FLUORESCENCE QUENCHING IODIDE-ION LIPOPEPTIDE LOCALIZATION LOSS SPECTROSCOPY EELS LYMPHOCYTES MARROW-DERIVED MACROPHAGES PEPTIDE-SYNTHESIS PEPTIDES VESICLEHAInteraction of Immunologically-Active Lipopeptides with Membranesu$Biochimica et Biophysica ActaE 11491 29-39 18 Jun 5088F?Metzler, W.J. Valentine, K. Roebber, M. Marsh, D.G. Mueller, L.o 1992Proton resonance assignments and three-dimensional solution structure of the ragweed allergen Amb a V by nuclear magnetic resonance spectroscopy Biochemistry3137 8697-8705 22 Sep 5087VPMetzler, W.J. Valentine, K. Roebber, M. Friedrichs, M.S. Marsh, D.G. Mueller, L. 1992zAMINO-ACID SEQUENCE CROSS-RELAXATION ELUCIDATION H 1 NMR NMR-SPECTROSCOPY POLLEN ALLERGEN PROTEINS RA5 SPECTRA SUPPRESSIONAnalysis of two-dimensional NMR experiments has afforded essentially complete assignment of all proton resonances in the allergenic protein Amb t V. Conformational constraints were obtained from the NMR data in three forms: interproton distances derived from NOE cross-peak intensities of NOESY spectra, torsion angle constraints derived from J-coupling constants of COSY and PE-COSY spectra, and hydrogen bond constraints derived from hydrogen-exchange experiments. Conformations of Amb t V with low constraint violations were generated using dynamic simulated annealing in the program XPLOR. The refined structures are comprised of a C-terminal alpha-helix, a short stretch of triple-stranded antiparallel beta-sheet, and several loops. In addition, the cystine partners of the four disulfide linkages (for which there are no biochemical data) have been assigned. The refined structures of Amb t V will allow us to suggest surface substructures for the Amb V allergens that are likely to participate in B cell epitopes and will assist us in defining the Ia/T cell epitopes that interact with the MHC class II (or Ia) molecule and the T cell receptor leading to the induction of the immune response to Amb t V.|Determination of the 3-Dimensional Solution Structure of Ragweed Allergen Amb-t-V by Nuclear Magnetic Resonance Spectroscopy Biochemistry3122 5117-5127 9 Jun 5089vpMeunier, S. Bernassau, J.-M. Sabatier, J.-M. Martin-Eauclaire, M.F. Van Rietschoten, J. Cambillau, C. Darbon, H. 1993$DISULFIDE NMR STRUCTURE TOXINztSolution Structure of P05-NH2, a Scorpion Toxin Analog with High Affinity for the Apamin-Sensitive Potassium Channel Biochemistry32 11969-11976 5091Meury, J. Kohiyama, M. 1991NHENCODED PROTEINS GENE GRPE INITIATION MEMBRANE REPLICATION STRESS SYSTEMPIRole of Heat Shock Protein DnaK in Osmotic Adaptation of Escherichia-ColidJournal of Bacteriologyr 17314 4404-4410n Jul`Daviess+ ss s s s}sg*g[gKg*gg!g+]gUg."g.)g/sg6gggnons/l lasws3y=y&yyrwwwwwwl l el 6l*l+#llssJsEsGsssoo ko so!so$o&o+o&o-3o.o1To1o4o8o9o9]o o+Zo oonsjsonletov2W Sahasrabudhe1993  Sahayamary19933X Sahintoth1993%6 Sahyoun1992Y Saibil1991 ' Saibil1992  Saibil19944 Saido1991 Saier1991 X Saier1992$ Saier1992% Saier1992 Saier1992#, Saier1993 Saier1993% Saijo1992Z Saint1993! Sainz1986\ Sainz1986[ Sainz1986l Sairyo1992 ] $R$A)A$A$A%A%A%A%A+*A% A%A%A%A%A%!A%$A%,A&A%6A%CA%JA%MA%OA%TA%eA%gA%fA%wA%yA%xA%{A%}A%A%A%A%A%A%A%A'WA%A%A%A%A%A%A%A%A%A%A%A%A%A%A%A%A&A&A&A&A&A&A&Aiiiii I' IIIII"IIING!'iburgere felder.re.QUQVQqmm m m m m m {mm3o-omm Amanz z z z zA tb t,tlyzeiiiii I' IIIIINGier felder.re.QUQVQQSoaaa)$aa)aaaGaMaTaa)a4amaaaaa^aaa=a)a)a&aaaa Ba Ea a a a a a a a a a a a a a!a!a!Qa!Pa)a!a" a"a"a)a#a)a)a)a)a)a)a)a)aelstein1991 n Finkelstein1991 m Finkelstein1991 Finkelstein1992 Finkelstein1992 r Finkelstein1993 q Finkelstein1993$ Finkelstein1993*N Finkelstein1997*  Finkelstein1997 Finlay19921*I Finley1997  Finn19919I Finn19931 Finnegan1990*" Finzel1989 Finzi1992  Fiol19901 s Fiordalisi1993 tFiorella1991Fiorella1991 Fiori1992 u Fiori1993 vFiorillo1992!Byt!a!a!a"a"2a"4a"Ma"va"xa"wa"ya"a"a"a"a#a#a)a#^a#qa#za#{a#a#a#a#a#a$&a)a$Qa$a$a$a$a$a%&a%a%a%a&a&/a&0a&Oa&_a&a&a)%a)&a)'a)5a)(a)+a)-a)1a))a)*a+Xa+\a+\a+\a+\a+\a+\ao To#o#o$ooOooo&x6xSxx xx yx -x x x' xx)xxxxx&xxxxxpx+ xIxxxxRxXxxx)x [s!s#zs#s&s&Os)%s)'s)-s+Xs'Js %sx u u'QudsenooBocurs Thus, the light-harvesting chlorophyll a/b-binding protein, cytochrome f, and the R ieske FeS protein all showed strong cross-linking products with 54CP. In contrast, no cross-linking to the 23- and 33-kDa proteins of the oxygen-evolving complex were detected. The selectivity of 54CP correlates with the hydrophobicity of the thylakoid-targeting si 5536<6Nicholson, H. Anderson, D.E. Daopin, S. Matthews, B.W. 1991rlBACTERIOPHAGE-T4 LYSOZYME BONDS DENATURATION MODEL MUTAGENESIS PH PROTEIN STABILITY RESOLUTION STABILIZATION It was shown previously that the introduction of a negatively charged amino acid at the N-terminus of an alpha-helix could increase the thermostability of phage T4 lysozyme via an electrostatic interaction with the "helix dipole" [Nicholson, H., Becktel, W. J., & Matthews, B. W. (1988) Nature 336, 651-656]. The prior report focused on the two stabilizing substitutions Ser 38 --> Asp (S38D) and Asn 144 --> Asp (N144D). Two additional examples of stabilizing mutants, T109D and N116D, are presented here. Both show the pH-dependent increase in thermal stability expected for the interaction of an aspartic acid with an alpha-helix dipole. Control mutants were also constructed to further characterize the nature of the interaction with the alpha-helix dipole. High-resolution crystal structure analysis was used to determine the nature of the interaction of the substituted amino acids with the end of the alpha-helix in both the primary and the control mutants. Control mutant S38N has stability essentially the same as that of wild-type lysozyme but hydrogen bonding similar to that of the stabilizing mutant S38D. This confirms that it is the electrostatic interaction between Asp 38 and the helix dipole, rather than a change in hydrogen-bonding geometry, that gives enhanced stability. Structural and thermodynamic analysis of mutant T109N provide a similar control for the stabilizing replacement T109D. In the case of mutant N116D, there was concern that the enhanced stability might be due to a favorable salt-bridge interaction between the introduced aspartate and Arg 119, rather than an interaction with the alpha-helix dipole. The additivity of the stabilities of N116D and R119M seen in the double mutant N116D/R119M indicates that favorable interactions are largely independent of residue 119. As a further control, Asp 92, a presumed helix-stabilizing residue in wild-type lysozyme, was replaced with Asn. This decreased the stability of the protein in the manner expected for the loss of a favorable helix dipole interaction. In total, five mutations have been identified that increase the thermostability of T4 lysozyme and appear to do so by favorable interactions with alpha-helix dipoles. As measured by the pH dependence of stability, the strength of the electrostatic interaction between the charged groups studied here and the helix dipole ranges from 0.6 to 1.3 kcal/mol in 150 mM KCl. In the case of mutants S38D and N144H, NMR titration was used to measure the pK(a)'s of Asp 38 and His 144 in the folded structures. These provide independent estimates, under different experimental conditions, of 1.4 and 0.9 kcal/mol in 100 mM KCl for the respective interaction energies in these two instances. NMR also indicates that the favorable electrostatic interaction energy for Asp 92 in wild-type lysozyme is approximately 2.1 kcal/mol. As evidenced by the mutants T109D, N116D, N144H, and N144D, electrostatic interactions between the second residue within an alpha-helix and the N-terminus appear to be especially important for stability. These results provide a rationale for the previous empirical observation that aspartic acid is the most commonly observed amino acid at this position while histidine is rarely observed [Richardson, J. S., & Richardson, D. C. (1988) Science 240, 1648-1652].Analysis of the Interaction Between Charged Side Chains and the alpha-Helix Dipole Using Designed Thermostable Mutants of Phage T4-Lysozymei Biochemistry3041 9816-9828 15 Oct^2203=333*3#3#3.39]99E9e9 9 9 9 `99999999999!9#9'9)%9)-9*99/9/ 91n92i9294Y949595969697979&992!2222(2G22 v2 2 2 .2 K2 2 W2 b2 2}22222/2222 %"%!2% %5%X%2,l%h% 8541,%Wittekind, M. Reizer, J. Klevit, R.E. 1990COHERENCE-TRANSFER DEPENDENT PHOSPHOTRANSFERASE SYSTEM ESCHERICHIA-COLI GRAM-POSITIVE BACTERIA HISTIDINE-CONTAINING PROTEIN NUCLEAR MAGNETIC-RESONANCE PHOSPHOCARRIER PROTEIN PHOSPHOENOLPYRUVATE SPECTROSCOPY TWO-DIMENSIONAL H-1-NMRSequence-Specific H-1 NMR Resonance Assignments of Bacillus-Subtilis Hpr - Use of Spectra Obtained from Mutants to Resolve Spectral Overlap1 Biochemistry2931 7191-7200  7 Augb 8540VOWittekind, M. Rajagopal, P. Branchini, B.R. Reizer, J. Saier, M.H. Klevit, R.E.l 1992HBCOUPLING-CONSTANTS DISTANCE GEOMETRY ESCHERICHIA-COLI GRAM-POSITIVE BACTERIA HISTIDINE-CONTAINING PROTEIN HPR NMR NUCLEAR MAGNETIC-RESONANCE PHOSPHOENOLPYRUVATE PHOSPHOTRANSFER PORCINE PROCARBOXYPEPTIDASE-B PROTEIN-STRUCTURE SUGAR PHOSPHOTRANSFERASE SYSTEM SUGAR TRANSPORT SYSTEM TERTIARY STRUCTURE TWO-DIMENSIONAL H-1-NMRtmSolution Structure of the Phosphocarrier Protein HPr from Bacillus-Subtilis by 2-Dimensional NMR SpectroscopyIProtein ScienceH110 1363-13760 Oct Wittekind, M. Mueller, L. 1993HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the a- and b-carbon resonances in proteins h i o p $Journal of Magnetic Resonanceg B101201-205B jlf1 8542 Wittinghofer, A. Pai, E.F. 1991b[ACTIVATING PROTEIN BINDING DOMAIN GAP GDP GTP HYDROLYSIS HA-RAS IDENTIFICATION MEMBRANE P21NGThe Structure of Ras Protein - A Model for a Universal Molecular SwitchR$Trends in Biochemical Sciences1610382-387I Oct 85432+Wittka, R. Stocker, M. Boheim, G. Pongs, O.e 1991b[BRAIN CDNA DIVERSITY DROSOPHILA MUSCLE GENE LOCUS POLYMERASE CHAIN-REACTION XENOPUS OOCYTESnhMolecular Basis for Different Rates of Recovery from Inactivation in the Shaker Potassium Channel Family FEBS Letters 286 1-2R193-200 29 Jul127185354217 2003 May 6hPJThe J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp704937-44'TNDepartment of Chemistry, Tulane University, New Orleans, Louisiana 70118, USA.B;Wittung-Stafshede, P. Guidry, J. Horne, B. E. Landry, S. J.a("22604629 0006-2960 Journal Article Biochemistrylehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12718535n("Wlodawer, A. Savage, H. Dodson, G. 1989JCStructure of insulin: results of joint neutron and X-ray refinementActa Crystallographica45 (( Pt 1))  99-107 1 Feb 8544 85454-Wodak, S.J. Lasters, I. Pio, F. Claessens, M.  1990b[Basic design features of the parallel alpha beta barrel, a ubiquitous protein-folding motif"Biochemical Society Symposia57 99-121Wofsy, C. Goldstein, B. 2002rlEffective Rate Models for Receptors Distributed in a Layer above a Surface: Application to Cells and Biacore Biophys J824 1743-1755 11916835http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11916835 http://www.biophysj.org/cgi/content/full/82/4/1743 http://www.biophysj.org/cgi/content/abstract/82/4/1743'hbDepartment of Mathematics and Statistics, University of New Mexico, Albuquerque, New Mexico 87131. 8546VPWolber, V. Maeda, K. Schumann, R. Brandmeier, B. Wiesmuller, L. Wittinghofer, A. 1992ESCHERICHIA-COLI FUSION PROTEINS GLUTATHIONE S TRANSFERASE HYBRID PROTEINS LIGHT-MEROMYOSIN PLASMID VECTORS SKELETAL-MUSCLE MYOSIN STEP PURIFICATION TAT PROTEIN VIRUS TYPE-IIINleA Universal Expression-Purification System Based on the Coiled-Coil Interaction of Myosin Heavy Chain-108900-9041 Aug0 Biotechnology0 8550Wolf, G. Zerlauth, G. 1988JDTumor promotion, vitamin A, and fibronectin. A review of recent work 259201-216T2,Progress in Clinical and Biological Research6D626262626262727272727 2727272727+27.27/27027127227;27<27G27Q27\27^27`27a27c27f27i27o27q27t27w27x27y27}27272727272727272727272727272727272727272727272728qa8wa8}a8~a8a8a8a8a8a8a8a8a8a8a#aaaa27a7a7a7a7a7a7a7a7a7a7a7a7a#aaaa2 `@@7Has7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a7a ESCHERICHIAs i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i0 i1 i# i i)/ i0 i0 i+  iz i0 i0 i5 i5 i5 i6 i63 i6= i6@ i6D i6G i6K i6O i6f i6y i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i6 i7 i7 i7" i7# i7' i7, i7. i73 i75 i76 i6P6262626262626262626262626262626262626262626262626272727 27272727"27(27.27527627G27I27N27O27Z27_27`27b27h27m27o27t27x272727272727272727272727272722Y2233/353:3>3A3Q23`3U3l/j3333 3333333333434l4l4#l4(l48l44l4;l4H4G4M4Q4p4x44{444s443i4144 54 5G5d5c}5b}5`}5_}5o}ngeneticsoOsOrOO#O*OOOOOOOOO1O5ONOXOeOOO]O_OOOOOO\OOQOSOOO O O O O O!O!yO!O"O"[O"^O"uO"O"O"O"O#O##O#JO#SO#VO#iO#O#O#O#O#O$$Ooteins: Structure, Function and Genetics*$Islam, S.A. Karplus, M/ Weaver, D.L. 2002`ZApplication of the diffusion-collision model to the folding of three-helix bundle proteins"Journal of Molecular Biology 318199-215 JAH 3462 Ismail, A.A. Mantsch, H.H. 1992:3CHARGE PEPTIDES POLY L LYSINE PROTEINS SPECTROSCOPYCRLSalt Bridge Induced Changes in the Secondary Structure of Ionic Polypeptides Biopolymersa329 1181-1186 Sepezd^ v'En 1456"Creighton, T.E. Darby, N.J.B 1989VOFunctional evolutionary divergence of proteolytic enzymes and their; inhibitors$Trends in Biochemical Sciences148319-324 Aug 1455"Creighton, T.E. Chothia, C.r 1989:3Protein structure. Selecting buried residues [news]p Nature 339o 6219 14-15 4 MayCreighton, T.E. 1990Protein FoldingBiochemical Journal< 270  1-16Review ArticleSJE JAH  Creighton, TE 1990Protein Structure Rickwood, D Hames, BDPractical Approach  Oxford, UK Oxford University Press orange bookCreighton, T.E. 1991 Unfolding protein folding. Nature 352 17-18d SJECreighton, T.E. 199160Characterizing intermediates in protein folding.Current Biology1 8-10Creighton, T.E. Kim, P. 1991Folding and bindingd,%Current Opinion in Structural BiologyP1 3-4  1462Creighton, T.E. 1991(!Stability of folded conformations,%Current Opinion in Structural Biology1 5-16 1445 1444Creighton, T.E.4 1991 GROEL MOLTEN-GLOBULE STATE60Molecular Chaperones - Unfolding Protein Folding Nature 352L 6330 17-18 4 JulCreighton, T.E. 1992.'The disulphide folding pathway of BPTI.Science  256111-112  1448Creighton, T.E.4 19924.The disulfide folding pathway of BPTI [letter]ScienceC 256 5053111-114f 3 Apr 1447Creighton, T.E.4 1992RKCYSTEINE-14 INTERMEDIATE LACKING MUTANT PANCREATIC TRYPSIN-INHIBITOR THIOLSO,%The Disulfide Folding Pathway of BPTI Science 256t 5053111-112 3 Apr 1446Creighton, T.E.4 1992xrCRYSTAL-STRUCTURE ESCHERICHIA-COLI EXPRESSION MODEL PLASMINOGEN-ACTIVATOR INHIBITOR PRO-SEQUENCE REGION SUBTILISIN.(Protein Folding - Up the Kinetic Pathway Nature 356L 6366194-195 19 MarCreighton, T.E. 1992Protein Folding New York W.H. Freeman & Co.Creighton, T.E. 1992Up the kinetic pathway. Nature 356194-195Creighton, T.E. 1992Folding and binding.2 1-5,%Current Opinion in Structural Biology, 1452`YCreighton, T.E. Bagley, C.J. Cooper, L. Darby, N.J. Freedman, R.B. Kemmink, J. Sheikh, A.m 1993ENDOPLASMIC-RETICULUM ESCHERICHIA-COLI GEL-ELECTROPHORESIS GONADOTROPIN BETA SUBUNIT LUMINAL ER PROTEINS NMR-SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE ORGANELLE TARGETING PATHWAY PROTEIN DISULFIDE ISOMERASE PROTEIN DISULPHIDE ISOMERASE RIBONUCLEASE-A SIGNAL PEPTIDE PROCESSINGOn the Biosynthesis of Bovine Pancreatic Trypsin Inhibitor (BPTI) - Structure, Processing, Folding and Disulphide Bond Formation of the Precursor Invitro and in Microsomesp 232p4 1176-1196 20 Aug"Journal of Molecular Biology 1451Creighton, T.E.4 1993@9Protein Folding Pathways Determined Using Disulfide Bonds0 Bioessays014195-199rCreighton, T.E. 19936/Proteins. Structures and Molecular Properties.  New York, NY Freeman, WH and Company 2nd  1449"Creighton, T.E. Ewbank, J.J. 1994EX PERS RIFAI PEPTIDE CONFORMATIONS RELAXATION MATRIX APPROACHComplexation and Medium Effects on the Conformation of Cyclosporin-A Studied by NMR Spectroscopy and Molecular Dynamics CalculationsBiochemical Pharmacology401169-173 1 Jul 3850("Kessler, H. Anders, U. Schudok, M. 1990AMINO-ACIDS BIOLOGICAL-ACTIVITY COUPLING-CONSTANTS DIMENSIONAL NMR-SPECTROSCOPY HETERONUCLEAR CORRELATION SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE ROTATING-FRAME SEQUENCE SHIFT CORRELATION SPECTROSCOPY SOMATOSTATIN|vAn Unexpected Cis Peptide Bond in the Minor Conformation of a Cyclic Hexapeptide Containing Only Secondary Amide Bonds.(Journal of the American Chemical Society 11216 5908-59166 1 Aug 3855>7Kessler, H. Mronga, S. Muller, G. Moroder, L. Huber, R. 1991COHERENCE-TRANSFER CYCLIC SOMATOSTATIN ANALOG FRAGMENT HETERONUCLEAR MOTION NUCLEAR MAGNETIC-RESONANCE PROTEIN-STRUCTURE RESOLUTION ROTATING-FRAME SPIN COUPLING-CONSTANTSThe hinge region links the antigen binding F(ab) part to the constant F(c) domain in immunoglobulins. For the hinge peptide derivative [AcThr (OtBu)-Cys-Pro-Pro-Cys-Pro-Ala-ProNH2]2 the assignment of the H-1 and C-13 resonances was achieved by two-dimensional nmr techniques: total correlation spectroscopy (TOCSY), nuclear Ovethauser enhancement spectroscopy (NOESY), rotating frame nuclear Overhauser enhancement spectroscopy (ROESY), heteronuclear multiple quantum coherence (HMQC) transfer, and a HSQC (modified Overbodenhausen experiment) with high resolution in F1, which was several times folded in F1 but still phase correctable. Conformational relevant parameters (78 nuclear Overhauser effect distance restraints, 3J(HH) for prochiral assignments, temperature gradients) were determined by nmr and served as input data for molecular dynamics (MD) structure refinement. A simulated model compound corresponding to the [Cys-Pro-Pro-Cys]2 core elongated by the peptide chains in the F(ab) and F(c) direction served as a starting structure for the final MD run. The conformation calculated in in vacuo does not agree with the C2 symmetry required from nmr data, but the structure obtained by a water simulation fulfills the requirement. Here the core of the hinge peptide derivative adopts a polyproline II double helix as in the x-ray structure of IgG1. Hence, segments responsible for the internal flexibility are located outside the core as confirmed by the flexibility of the solvent exposed C termini.Conformational Analysis of a IgG1 Hinge Peptide Derivative in Solution Determined by NMR Spectroscopy and Refined by Restrained Molecular Dynamics Simulations Biopolymers3110 1189-1204 Sep.*zindistinguishablev!v"wv8Dv&vidualu u og l  l  l c l& l l l l l( l l l l " l$E l&I l' l* l, l( l* l- l0 l0 l l[ l$L l6 l7 l l l l~ l  l l l l!4 l"M l# l+ l  l? l$ l~ l' l l l^ l l& l"M l"y l#q l# l&/ l)* l+ l/M)/)i0+)xytuvw"#'#&#$#%-s/00.=//e0 0 0 M)0000000000"0$0&0(0/0007090=0?0E0E0EE0E0E0E00E~ Jardetzky r u pR j jZ j&U j+ j6iwala)jour*p+nik4Xoniec7s7s,sik-ppp4per/rcrrelle>e e e ye%t :tts0s1sv4bo-old6lv2vis'Ps5a9-a3anoff4c6c7c cur8C#EPs#u$Ckolski+wal1t6t+tzkeuussim/var/y1|y2My5I'y9R achandran9ram:an; C, b0b0c0c0c0c1Fc/c 21171731728241420193|85633|9 9203$3%)333}09783}432+{41:5411:77927981800191i9631i76f650836f71975483193$327 4 44331]3Y338261583 312493124 4/40U42K0032K527527975405785818977941844y6n68241420193|85633|9 9203$3%)333}09783}432+{41:5411:77927981800191i9631i76f650836f71975483193$327 4 44331]3Y338261583 312493124 4/40U42K0032K527527975405785818977941844y6n6     6 7 W X  Nature Structural Biology310868-873SJE JAHHamada, D. Goto, Y.  1997TThe equilibrium intermediate of b-lactoglobulin with non-native a-helical structure.   ! @ A "Journal of Molecular Biology 269479-487 SJE^R NonBONDED c c c c ce c c c c  c#  c# c# c# c$ c  c$G c7qranched catalytic l6" lSlassicale e e e{eaved7 okodedIING  M8gnitive73 incidence)(mpactETITIVE6"n ' nservativev.valentiN operative ii b ity8qupledvalentX e X l Y lM l l F l%a l+ l/ l0U l2 lX l l$ l+q l6> l7; l8} l8 l  lyr! r- r7 rystallinityh$ ographics ytoplasmicad"xd(dementedn& n!D naturatingn edl# ing# t7; t8 t tectableiisulfide"e" " 7 ?N ?N?Nrystallographic ytoplasmicead(dementedd& n!D naturatingn edl tectabledisulfide?e?e75G7>27I27R27]27_27`27h27r27u27v27{27|27272727272727272727272727272727272727272727282828 2828282828$28)28*28,28028628828?28C28F28G28N28R28T28Z28f28v28|28282828282828282828282828282829292929729?29H29G29R282729W29j2`2_2^2]27272727272727272727282828 28272828282828$28)28*28,28028628828?28C28F28G28N28R2`2_2^2]22. 0 Simulation / s  s  s  s  s  s  s  s  sc s` s1 sG sh sj si s s s s s s s s, s s s s( s s s1 s s s s s s s_ sS s sd s s s @ s u s!t s! s" s"E s" s" s" s# s% s& s& s& s'J s+ s  s s+ s+ s/ s/ s/ s/ s5 s6 s68 s6H s6e s6 s6 s6 s6 s6 s7 s8$ s8; s8I s8d s8e s8j s8n s8p s8 sC s s s s6H s6b s6e s7 s7 s84 s8; s$ s s s_ sS s sd s s s @ s u s!t s! s" s"E s" s" s" s# s% s& s& sC s s s s$ ss"HMoDel"I"I"I"I#I#`I#aI#I$ I*JI$$I$)I$JI$I$I)I%I%.I%aI%I%I%I%I&I&I& I&CI&BI&gI&fI&rI&wI&sI&I&I'KIHI+II,/I,KIoI,RI,\I(I,I I)I CI-NI-I-I.#I.$I.AI.I.II&I'SI(I/FI(X&9E&AE&@E&?E&HE&UE&bE&E&E+E+E+E+E+E)E|E+AE{EEEaE*sE*tE*uE E,aE*E)E,eE,E,E*0E E,E-,E&}EqE-5E-`E,E-E.EEEEE+DE.E.E.E.E.E.E.EE/E/=E/nE/dE.E/E/E/Etz, T.A. 2003lfStructures of five antibiotics bound at the peptidyl transferase center of the large ribosomal subunit"Journal of Molecular Biology 330E 1061-1075E KSR 29824.Hanson, M. Unger, K.K. Mant, C.T. Hodges, R.S. 1992XRALPHA-TROPOMYOSIN AMINO-ACID SEQUENCE HALF MODEL PERFORMANCE LIQUID-CHROMATOGRAPHYPolymer-Coated Reversed-Phase Packings with Controlled Hydrophobic Properties .2. Effect on the Selectivity of Peptide Separations Journal of Chromatographys 599 1-2. 77-85. 22 May 29814.Hanson, M. Unger, K.K. Mant, C.T. Hodges, R.S. 1992haCOMPONENTS PEPTIDES PERFORMANCE LIQUID-CHROMATOGRAPHY PURIFICATION RETENTION TEMPERATURE TROPONINuPolymer-Coated Reversed-Phase Packings with Controlled Hydrophobic Properties .1. Effect on the Selectivity of Protein Separations Journal of Chromatographys 599 1-2g 65-75 22 MayHanssens, I. Baert, J. 1991|uInfluence of Mg2+ and Inorganic Phosphates on the Assembly of Tubulin Depleted of Its Exchangeable Guanine Nucleotiden Biochemistry243d535-5410 Jun 2983D=ABSENCE ATP BINDING GTP ANALOGS MAGNESIUM POLYMERIZATION SITE 2984.'Hanzlik, R.P. Jacober, S.P. Zygmunt, J. 1991}ANALOGS CATALYZED HYDROLYSIS CYSTEINE PROTEINASES INHIBITION KINETIC SPECIFICITY MECHANISM NMR PROTEASES SERINE THIONO ESTERSZTReversible Binding of Peptide Aldehydes to Papain -Structure- Activity Relationships$Biochimica et Biophysica Acta 10731C 33-42 23 Jan:3Hao, M.H. Pincus, M.R. Rackovsky, S. Scheraga, H.A. 1993|vUnfolding and refolding of the native structure of bovine pancreatic trypsin inhibitor studied by computer simulations Biochemistry3237 9614-9631  21 Sep 2985BETA-SHEET ENERGY PARAMETERS HYDROGEN-BOND INTERACTIONS MAGNETIC-RESONANCE DATA MODEL MOLECULAR-DYNAMICS MONTE-CARLO NONBONDED INTERACTIONS OCCURRING AMINO-ACIDS PROTEIN CONFORMATION Hao, M. -H. Scheraga, H.A. 1998:3Theory of Two-State Cooperative Folding of Proteins$Accounts of Chemical Research318433-440 JAHs Hao, M.-H. Scheraga, H.A.  1998>8Molecular Mechanisms for cooperative folding of proteins"Journal of Molecular Biology 277973-983d JAHe0*Haque, T. S. Little J. C. Gellman, S. H. 1996.(Journal of the American Chemical Society 118 6975&5587 7 7'7 d7 :7l7w777!7-7A777"7#7#7&7{77)F72.78 7770!f0+g0+0608040)01 11L1M3.3k3a0&G0-0-0/01,0+070I0! 011,:23 >3445)/5e66U647881[91[91[91[922BIole25o26o27o2;o2=o2?o2Io2Go2Jo2Ko2Mo2Qo2[o2\o2]o2_o2`o2jo2mo2po2qo2so2wo2yo2|o2}o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o1jo2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o2o3Gov3 '3"'3#'3$'3%'3&'3'3'3''3('3)'3*'3+'3,'3-'3.'3/'30'31'32'33'34'35'36'3:'39'38'37'3@'3;'3<'3='3>'3?'3'3P'3O'3N'3K'3L'3M'3S'3R'3Q'2'3'3f'3e'3d'3c'3b'3a'3`'3_'3^'3]'3\'3['3Z'3Y'3X'3W'3W'3PNIH3Oe3Ne3Ke3Le3Me3Se3Re3Qe2e3e3fe3ee3de3ce3be3ae3`e3_e3^e3]e3\e3[e3Ze3Ye3Xe3We3Ve3Ue3le3re3ve3me3qe3we3se3ke3te3ue3oe3ne3xe3je3pe3ze/e3{e3|e3}e3~e3e3e3e3e3e3e3e3e3e3e3e3e3e3e)N0a0a/a/a0a0!a0)a*a0-a04a0<a0Da0Ea0Fa0Ga0Ia0Ha0Va0Za0Ma0na0ra0ua0a0a0a0a0a0|a0a1a1a&]a0`a"a0a"a1(a1a0gala0a14a18a1Ca1Oa1Xa1Za1pa1a1a1a1a1a1a1a1a1a1a1a1a1a1a7 a.-e pphin, human growth hormone, human epidermal growth factor and superoxide dismutase, and mouse-human Fab proteins, and novel approaches for secretion of foreign proteins. The effects of host strain, growth temp., length of induction, and cotranscription 1512Cyr, D.M. Douglas, M.G. 1991ADP-ATP CARRIER ATP BETA-SUBUNIT PRECURSOR ESCHERICHIA-COLI INNER MEMBRANE MATRIX OUTER-MEMBRANE PROTEIN RECEPTOR TRANSLOCATION YEAST MITOCHONDRIA \ UStudies with a synthetic presequence peptide, F1-beta-1-20, corresponding to the NH2-terminal 20 amino acids of the F1-ATPase beta-subunit precursor (pF1-beta) show that although this peptide binds avidly to phospholipid bilayers it does not efficiently compete for import of full-length precursor into mitochondria, K(i) approximately-equal-to 100-mu-M (Hoyt, D. W., Cyr, D. M., Gierasch, L. M., and Douglas, M. G. (1991) J. Biol. Chem. 266, 21693-21699). Herein we report that longer F1-beta presequence peptides F1-beta-1-32 + 2, F1-beta-1-32SQ + 2, and F1-beta-21-51 + 3 compete for mitochondrial import at 1000-, 250-, and 25-fold lower concentrations, respectively, than F1-beta-1-20. A longer peptide, F1-beta-1-51 + 3, was no more effective as an import competitor than F1-beta-1-32 + 2. Both minimal length and amphiphilic character appear required in order for F1-beta-peptides to block mitochondrial import. Import competition by longer F1-beta-peptides seems to occur at a step common to all precursors since they blocked import of precursors to F1-ATPase alpha- and beta-subunits and the ADP/ATP carrier protein. Dissipation of membrane potential (DELTA-psi) across the inner mitochondrial membrane is observed in the presence of F1-beta-peptides, but this mechanism alone does not account for the observed import inhibition. F1-beta-1-32 + 2 and 21-51 + 3 block import of pF 1-beta 100% at peptide concentrations which dissipate DELTA-psi less than 25%. In contrast, experiments with valinomycin demonstrate that when mitochondrial DELTA-psi is reduced 25% import of pF1-beta is inhibited only 25%. Therefore, at least 75% of maximal import inhibition observed in the presence of F1-beta-1-32 + 2 and F1-beta-21-51 + 3 does not result from dissipation of DELTA-psi. Import inhibition by F1-beta-peptides is reversible and can be overcome by increasing the amount of full-length precursor in import reactions. F1-beta-presequence peptides and full-length precursor are therefore likely to compete for a common import step. Presequence dependent binding of pF1-beta to trypsin-sensitive elements on the outer mitochondrial membrane is insensitive to inhibitory concentrations of F1-beta presquence peptide. We conclude that import inhibition by F1-beta-presequence peptides is competitive and occurs at a site beyond initial interaction of precursor proteins with mitochondria.voEarly Events in the Transport of Proteins into Mitochondria - Import Competition by a Mitochondrial Presequenceh&Journal of Biological Chemistrye 266 32 21700-21708  15 Nov2METhodOssss 1s xs s vs s s(s s s s s /s s sss>ssss ss(ssssss-srssNsssussss Rs Ts s"$s"s#s$s$s%s&s+Ms+s+s, s%ss-s.zs/s.s/s$s0s1s1s1ss1s28s2s39s3bs3s47s4s'Zs5Os5s6Ys6{s6s71s7s8s8s8s9s9s9s9s9 s9)s9Us8syssso" s) s#q s+i s+q sTs'tt t t t wttSttbt`t tt0tStmt!4t#t$t$St0 accessibility5 t6 t6E t6v t6 t6 t7p t7 t7 t8 t.W tyle o o& o# o% o* o o o. o4r o4 ow o  o  o oX o o o o# o$< o$= o- o& o < o o o o#{ o)+ o'Q o- o+Y o6 o6! o6E o6` o6g o6 o6 o7i o7l o7p o7 o7 o8d o8 o8 o8 o8 oory o o2~ o o o o8. o\ommodated+t d4) d5 d6 d  d69 sh s$ ingG on  o9` o6M oodationpaniedg uU u) y y x y p y y Y%& Y6M s6b s6 s7P s8 s8 s+j sY  i  ing  rc r r r r r r& R&A&A&A&A&A&A&A&A&#A&,A&1A&4A&7A&CA&BA&OA&TA&VA&[A&eA&hA&gA&fA&A&A&tA&sA&yA&{A&A&A&A&A&A&A&A&A'A+HA+LA+SA+WA)3A))A)!A+AuA+aA'LAAAA)EA+hA*A A* A* A* A* A* A* A* A % 1 0 n 5 ` @ a  # In t o o  i a O2 ^ ' Q IR i    ro r       L l} S  ; c  s  s$j s$u $ %g Z& H q F/ o N # ' $ & % 1 0 n 5 ` @ a  # In t o o  i a O2 ^ 'H H %T'Wa%a%a%a%a%a%a%a%a%a%a(a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a%a&a& a& a&a&a&0a&Da&;a&Ka&Ja&Ra&_a&ca&da&xa&va&ua&a&a&a&a&a&a&a&a&a&a'!a'"aVX^~ContainsPlaxco 5683\UOhno, Y. Segawa, M. Ohishi, H. Doi, M. Kitamura, K. Ishida, T. Inoue, M. Iwashita, T. 1993ANALOGS BINDING COMPUTER-SIMULATIONS DELTA-OPIOID RECEPTOR DERMENKEPHALIN DERMORPHIN FEATURES MESSAGE-ADDRESS CONCEPT PEPTIDES SELECTIVITYConformation of Deltorphin-II in Membrane Environment Studied by 2-Dimensional NMR Spectroscopy and Molecular Dynamics CalculationsN& European Journal of Biochemistry 212y1185-191 15 Feb 5685NHOhta, Y. Hojo, H. Aimoto, S. Kobayashi, T. Zhu, X. Jordan, F. Inouye, M. 1991~xALKALINE PROTEASE INHIBITOR BINDING BPN COMPLEX ESCHERICHIA-COLI INVITRO S-SI SEQUENCE STREPTOMYCES-ALBOGRISEOLUS S-3253voPro-Peptide As an Intermolecular Chaperone -Renaturation of Denatured Subtilisin-E with a Synthetic Pro-PeptideMolecular Microbiology56 1507-1510 Jun 5686B;Ohta, Y. Kawato, S. Tagashira, H. Takemori, S. Kominami, S.h 1992vpDynamic Structures of Adrenocortical Cytochrome-P-450 in Proteoliposomes and Microsomes - Protein Rotation Study Biochemistry3150 12680-12687c 22 Dec 5684:3Ohta, T. Honda, K. Kuroda, M. Saito, K. Hayashi, H. 1993>7CLONING PENICILLIN BINDING PROTEIN PLASMID DNA SEQUENCEaMolecular Characterization of the Gene Operon of Heat Shock Proteins HSP60 and HSP10 in Methicillin-Resistant Staphylococcus-Aureus:3Biochemical and Biophysical Research Communicationsd 193e2730-737 15 Jun 5687*$Ohtaka, C. Nakamura, H. Ishikawa, H. 1992APHID ENDOSYMBIONT BACTERIAL ENDOSYMBIONT-SPECIFIC PROTEIN GENE-PRODUCTS HEAT-SHOCK PROTEINS IDENTIFICATION MITOCHONDRIAL PROTEIN PEA APHID PLANT RIBULOSE BISPHOSPHATE CARBOXYLASEyStructures of Chaperonins from an Intracellular Symbiont and Their Functional Expression in Escherichia-Coli groE MutantsJournal of Bacteriologyt 174c6 1869-1874 Mare 5689Ohtsuka, K. Laszlo, A. 1992CHINESE-HAMSTER FIBROBLASTS EXPRESSION MAMMALIAN-CELLS MOUSE HSP70 GENE NUCLEAR NUCLEOLAR LOCALIZATION SEQUENCE SHOCK PROTEINS STRESS THERMOTOLERANCEkF@The Relationship Between hsp-70 Localization and Heat Resistance Experimental Cell Research 202u2507-518 Oct4 5688 Ohtsuka, K. 1993pj40-KDA PROTEIN CELLS ENDOPLASMIC-RETICULUM GENE NUCLEOTIDE-SEQUENCE SACCHAROMYCES-CEREVISIAE YEAST HOMOLOGZSCloning of a cDNA for Heat-Shock Protein-hsp40, a Human Homologue of Bacterial DnaJB:3Biochemical and Biophysical Research Communicationsr 1971r235-240h 30 Nov 5691 Ojcius, D.M. Young, J.D.E. 1991|uALPHA-TOXIN ANALOGS CHANNELS DAMAGE HEMOLYSIN LIPID BILAYERS MEMBRANES SEA-ANEMONE SECONDARY STRUCTURE STREPTOLYSIN-O XQCytolytic Pore-Forming Proteins and Peptides - Is There a Common Structural MotifP$Trends in Biochemical Sciences166225-229 Junn7"7747944i614a 1995 AprizsProtein aggregation kinetics in an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant gene 1220-5LEThe tendency of recombinant protein in bacteria to partition into soluble and insoluble forms is attributed, in general, to a kinetic competition between protein folding and aggregation. However, little experimental work has actually been performed in vivo on the kinetics and mechanisms of protein folding and aggregation. Results are presented here from radiolabeling experiments which monitored the kinetics of recombinant protein aggregation in actively growing cultures. The strain used was an Escherichia coli strain overexpressing a Salmonella typhimurium CheY mutant gene. The rate of CheY aggregation was found to be time dependent in that the tendency of CheY to aggregate was greater for newly translated molecules, i.e., those translated within the previous several minutes, than for molecules translated less recently. CheY protein molecules that were translated less recently continued to aggregate for several hours but at a lower rate. The movement of soluble CheY to the insoluble form was enhanced at elevated growth temperatures and inhibited by the presence of chloramphenicol. The latter observation suggests that ongoing translation facilitates the movement of soluble CheY to the insoluble form. The implications of these results for the mechanism of protein aggregation in vivo, i.e., inclusion body formation, are discussed.t'TNDepartment of Chemical Engineering, University of Delaware, Newark 19716, USA.Klein, J. Dhurjati, P.("95266801 0099-2240 Journal ArticleAppl Environ MicrobiolBacterial Proteins/*genetics/*metabolism Chloramphenicol/pharmacology Escherichia coli/*genetics/*metabolism Genes, Bacterial Inclusion Bodies/metabolism Kinetics Membrane Proteins/*genetics/*metabolism Mutation Protein Conformation/drug effects Protein Folding Recombinant Proteins/genetics/metabolism Salmonella typhimurium/*genetics Solubility Support, U.S. Gov't, Non-P.H.S. Temperaturejdhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=77479444Electrongiiiisiiiiii*iiiiii i i i i!i!.i!Ki!~i"mi"i"i"i"i#i#i$i%i&Oi+_i'Ji.'i/i5i6i69i6Yi6di6i7i7i7i7i7di7i8i8Giii i aiei&iiiii,i!Di"i$Qi+_i'Ji  Eisenberg  r ` r w r x r r r r r) r$ r/H r0/ r2 r2 r4u r6Q r6 r r rQhaber2man"Benger55ssernstein r- r.  r rling Pfelder7ner0Uthlerll llylwl5^l?llll{lJ)JzJNJJ^JtJJJ J J J&J J OJ Jf protein cross-links. Biochemistry17 1479-1484JDJohnson, E.R. Anderson, W.L. Wetlaufer, D.B. Lee, C.-L. Atassi, M.Z. 1978D>Formation of three-dimensional structure in protein fragments. 253 3408-3414&Journal of Biological Chemistry 3599 Johnson, C.M. Price, N.C. 1986vpThe susceptibility towards proteolysis of intermediates during the renaturation of yeast phosphoglycerate mutase 2362y617-620eBiochemical Journal$8438$94\55*2.2100$05v'15'1$12$7$3$4$5$6602467 7$88$9%9$5+5+65N55 25 50103B07d00$0$1$3%4$5N586$6$6 7$8$89N6$6/6777+3,?0 0600$0$1$23$7$4$5$6$7$8$9/7777z33306{00$0$1$2+3+4$4$4.5$6$627$878'J8+8.9$9$9 82n22N080&M0+0 0,0.00+0$1$1222n2 2+22N0800+0227t Structure7x s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s7 s8 s8  s s6 s8, s81 s89 s8: s8< s8? s8@ s8A s8C s8D s8E s8N s8O s8P s8Y s8Z s8[ s8] s8b s8f s8l s8m s8p s8q s8u s8| s8~ s8 s8 s8 s8 s8 s8 s8 s8 s8 s8 s8 s6 s8 s s s s s s s s" s# s) s# s7 s\ s) s d d d d7 s7 s7 s8 s8  s s6 s8, s81 s89 s8: s8< s8? s8@ s8A s8C s8D s8E s8N s8O s8P s8Y s s s s s s s s" s# s) s# s7 s\ s) s d d d)127000000'000e0 0 0#^0)+0%0'J0+}0+0606906}060606060707^080 000001801N0-z01u'042'04'05'06'07'08e'001/1/10U1,s111 &000E0<0X000Z1 1$U000000010)0)0000'000e0 0 0^#0+)0%0J'0}+0+060960V60}6060606060 00000810N10z-0u1'024'04'05'06'001/1/1U01s,111 &000E0<0X000Z1 1U$000000100)0 * *L (  j z.N" 4 Harris, R.K. Becker, E.D. 2002leNMR nomenclature: Nuclear spin properties and conventions for chemical shifts - IUPAC recommendations$Journal of Magnetic Resonance2 156323-326  JAH Harrison, S.C. Durbin, R. 1985HAIs there a single pathway for the folding of a polypeptide chain?tVOProceedings of the National Academy of Sciences of the United States of America 8212 4028-4030e Juno 3020 JAH Harrison, R.K. Stein, R.L. 1990Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: Evidence for the existence of a family of distinct enzymes Biochemistry2916 3813-3816 JAH  3018"Harrison, P.J. Roberts, G.W. 1991AGENT ALZHEIMERS-DISEASE BRAIN CREUTZFELDT-JAKOB DISEASE DIAGNOSIS FAMILIAL DEMENTIA GERSTMANN-STRAUSSLER SYNDROME INCUBATION PERIOD PRECURSOR SCRAPIE INFECTIONVPLife, Jim, But Not As We Know It - Transmissible Dementias and the Prion Protein$British Journal of Psychiatryi 158457-470o Apri 3019 Harrison, R.K. Stein, R.L. 1992BETA-DEUTERIUM BINDING-PROTEIN CATALYSIS CYCLOPHILIN FK-506 ISOMERASE LIQUID-CHROMATOGRAPHY PEPTIDES PROLINE ISOMERIZATION WATERRLMechanistic Studies of Enzymic and Nonenzymic Prolyl Cis-Trans Isomerization.(Journal of the American Chemical Society 1149 3464-3471 22 Apr 3017:3Harrison, J.L. Taylor, I.M. Platt, K. Oconnor, C.D. 1992ESCHERICHIA-COLI F-SEX FACTOR GENE NUCLEOTIDE-SEQUENCE OUTER-MEMBRANE PROTEIN PERMEABILITY PLASMIDS PORIN PURIFICATION RESISTANCESurface Exclusion Specificity of the TraT Lipoprotein Is Determined by Single Alterations in a 5-Amino-Acid Region of the Protein Molecular Microbiology6 19 2825-2832 Octa 3016^XHarrison, B.C. Marcheseragona, S.P. Gilbert, S.P. Cheng, N.Q. Steven, A.C. Johnson, K.A. 1993$ATPASE IDENTIFICATION MOTILITYXQDecoration of the Microtubule Surface by One Kinesin Head per Tubulin Heterodimeru Nature 362f 6415 73-75 4 Mar& Harrison, P.M. Sternberg, M.J.E. 1994piAnalysis and classification of disulphide connectivity in proteins. The entropic effect of cross-linkage 244`448-463"Journal of Molecular BiologyHarrison, C.J. 1997zJLa cage aux fold: asymmetry in the crystal structure of GroEL-GroES-(ADP)7 I @ Structure5D10 1261HBHarrison, P.M. Bamborough,P. Daggett,V. Pruisner, S.B. Cohen, F.E. 1997 The prion folding problem,%Current Opinion in Structural Biology7 53-59SJE JAH 5Citation5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5e5ephan in Bacteriophage T4 Lysozymes Biochemistry29 5276-5285 JAH 3014NGHarris, D.A. Huber, M.T. Vandijken, P. Shyng, S.L. Chait, B.T. Wang, R. 1993ACTIVATION AMYLOID PROTEIN CULTURED-CELLS GERSTMANN-STRAUSSLER SYNDROME MECHANISM PRECURSOR PROTEOLYSIS SCRAPIE-ASSOCIATED FORM SEPARATION TRUNCATED FORMShbProcessing of a Cellular Prion Protein -Identification of N-Terminal and C-Terminal Cleavage Sites Biochemistry324y 1009-1016y 2 FebXEE 4E E E!E!CE!E!E!E"?E"dE"eE"E"E"E"E"E#uE#E#E$_E$`E$E%E& E&E&E&IE&NE&E)%E+fE,EEE'EEqEE E/E/E/E4xE4tE%jE5E5E5E6E6E6 E6E6E6!E6'E63E6DE6QE6bE6dE6wE6E6E6E6E6E6E6E6E6E6E6E6E6E6E6E7RE7fE7tE7xE7~E7E7E7E7E7E7E7E7E8E8:E8;E8GE8YE8ZE8dE8jE8{E8E8E8E8E8E\EEqauaaa^a a V1 V15DBv5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5A5Astudies_y-y yy0y7yCyy^yTyyy Vy y y yy6y+ yyy&yyy&yyyyhyyyyyy y y{y yMyyy'yXyyyy%y)yy y y y!oy!y"yy#qy#zy#y#y%y&Oy)1y4Ande4ee4e *e/ye4e4e)e4e$e% e%he$e/e4e5e4e+e<e5e5e54e/e5<e5;e5=e5>e5Ae5Be5Ce5De5Ge5He5Me5Le5Pe5Re5Xe5We5Ve5\e5Ze5ce5`e5_e5le5ke5fe5oe5we5e5e5~e5}e5|e5{e5eTe5e5e5e5e Lengthgss us osss$sYsCsmsssss!es+s,s,s.s-s/~s/s07s08s0s2s5xs5s6s7+s7Bs7^sss sssssszs1s ,s s"s#s#sss1s?s{sus7sss qssEs5s6ssssss2rCGi2sM2vM2M2M2M2M2M2M2M2M2M2M2M2M2M2M2M2M2M1VM2M2M2M2M2M2M2M2M2M1>M2M2M2M2M2M2M2M2M2M2M2M2M2M2M2l3l3l3l3 l3/l34l3:l3@l3>l3Ol3Rl3l3l3lW3lX3lY3l\3l- PRotein- , *-l)R--"-#9F*',m? CF+ +%--(-)&)=,& ,-!+; UU- - - - - - - -  -- - -  -- eAcylvmaaaa>aaaaa#a%a'Qa-a0a3a3a+aa(a)aaa*aaaa Aa a ha)a Pa alaaayaaaa+ aaaa -a a a"a"a"a#a$a$a$0a$a%a&Ca'Qaa6 a7a7Ia7a7a7a7a&aea#a'Qa0a6a6a6a7a7a7aaset.ted5C5C5C,J,a,a,a,a,a,a,a+a,a,a,a,a,a,a,a,a-a- a- a#va- aaaa*a)Ra-a-a*0a-a-a-$a-%a-&aa*a'aaa?a Ca aa*yaa-a"aXa-)a)a]a-+a;a;a;aaaaaaaaa#ofc#/#0n)n#^n#qn#zn#{n#n#n#R##n#n#n$&n)n$Qn$Un$|R$$n$n$n$n%n%&n%'n%n%%n%n%n&&/n&0n&On&_n&&n)n)%n)&n)'n)6n)5n)(n)+n),R)-R)1i))i)*+Xn+Zn+[i+\+n+^n+^n+^n+^n+^n+^n5Uids35o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o5o6o6o6o6o6o6o6o6o6o6 o6 o6 o6 o6o6o6o6o6o6o6o6o6ocripps.edu Kelly, J. W. Balch, W. E.eHB22628147 0021-9525 Comment Journal Article Review Review, Tutorial J Cell BiolAmyloid/*metabolism Animal Bacterial Proteins/metabolism Eukaryotic Cells/*metabolism Human Melanosomes/*metabolism Microfibrils/*metabolism Peptide Fragments/metabolism Prokaryotic Cells/*metabolism Protein Foldinglehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12743097Science, Rehovot, Israel. synthesized with a defe5' DEpartmentU5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s5' s6' s6' s6' s6' s6 ' s6 ' s6' s6' s6' s6' s6' s6' s6"' s6#' s6%' s6&' s6(' s62' s64' s64' s  : /1  j )I  7514"Stephan, Z.F. Yurachek, E.C. 199325OH-CHOLESTEROL BINDING CELL LINE HEP-G2 CULTURED HUMAN-FIBROBLASTS DEGRADATION FLUORESCENT HEPG2 CELLS HOMOZYGOUS FAMILIAL HYPERCHOLESTEROLEMIA INVITRO LOVASTATIN LOW-DENSITY LIPOPROTEIN MACROPHAGES SURFACE DiI-LDL (3,3'-dioctadecylindocarbocyanine-low density lipoprotein) has been extensively used in morphological and microscopic studies of receptor-mediated metabolism of LDL in many cell lines. To date the use of this fluorescent probe in a quantitative assay of LDL receptor activity has not been widely used in studies with multiple samples due to the lack of a practical method for quantitatively recovering cell-associated DiI. Therefore, detection by I-125-labeled LDL has remained the method of choice for assaying LDL receptor activity rapidly and reliably. In this paper, we describe a rapid, simple, and nonradioactive assay of LDL receptor activity using Dil-LDL. The increased sensitivity of this method was achieved by modifications to the labeling procedure of LDL and to the extraction of DiI from cells for subsequent fluorescence determination. These modifications did not affect the affinity of DiI-LDL toward HepG2 cells, and the assay was easily adapted to a rapid screen for LDL receptor modulators in this cell model. JDRapid Fluorometric Assay of LDL Receptor Activity by DiI-Labeled LDL Journal of Lipid Research342325-330 Feb.Stephens, C. Shapiro, L. 1997B;Bacterial Protein Secretion - A Target for New Antibiotics?Chemistry and Biology4p637-641 JLF 7515"Stephenson, R.C. Clarke, S.9 1992CYSTEINE FARNESYL IDENTIFICATION LAMIN-B MEMBRANE-BINDING DOMAIN METHYL ESTERIFICATION P21RAS PRODUCT SACCHAROMYCES-CEREVISIAE TRANSFERASECharacterization of a Rat Liver Protein Carboxyl Methyltransferase Involved in the Maturation of Proteins with the -CXXX C-Terminal Sequence Motif&Journal of Biological Chemistryo 267t19 13314-13319d 5 Jul 7517Stern, L.J. Wiley, D.C. 1992B-CELL LINE BINDING ENDOGENOUS ANTIGEN ENDOPLASMIC-RETICULUM HISTOCOMPATIBILITY ANTIGENS HLA IA INVARIANT CHAIN MOLECULES T-CELLS0ztThe Human Class-II MHC Protein HLA-DR1 Assembles as Empty alphabeta-Heterodimers in the Absence of Antigenic Peptide Cell683465-477 7 Febx 7516& Stern, B.D. Wilson, M. Jagus, R. 1993CAP BINDING PROTEIN CLEAVAGE ESCHERICHIA-COLI INHIBITOR MESSENGER RNA TRANSLATION PHOSPHORYLATION SITE PREVENTS PURIFICATION SEA-URCHIN EGGS SYSTEMS~wUse of Nonreducing SDS-PAGE for Monitoring Renaturation of Recombinant Protein Synthesis Initiation Factor, eIF-4-alphaX*#Protein Expression and Purification 44320-327 AugSternberg, N.J. 1973Properties of a mutant of Escherichia coli defective in bacteriophage lambda head formation (groE). II. The propagation of phage lambda"Journal of Molecular Biology76 25-44 7518JCSternberg, M.J. Hayes, F.R. Russell, A.J. Thomas, P.G. Fersht, A.R. 1987LEPrediction of electrostatic effects of engineering of protein chargesN Nature 330 6143 86-88I5-11 Nov 7519Sternberg, M.J.E.9 1990ztAMINO-ACID SEQUENCE ANTIGEN CDNA IMMUNOGLOBULIN MEMBRANE MOLECULAR-CLONING NUCLEOTIDE-SEQUENCE PROTEINS RAT RECEPTORRLInter-Species Sequence Conservation of Single-Spanning Transmembrane RegionsProtein EngineeringA4r1 45-47A Oct 7520XRSternlicht, H. Farr, G.W. Sternlicht, M.L. Driscoll, J.K. Willison, K. Yaffe, M.B. 1993tmCULTURED-CELLS CYTOSOLIC CHAPERONE MOLECULAR CHAPERONE PROTEIN PROTEIN FOLDING PULSE CHASE STUDIES RING TCP-1VPThe t-Complex Polypeptide-1 Complex Is a Chaperonin for Tubulin and Actin Invivo9020 9422-94260 15 OctVOProceedings of the National Academy of Sciences of the United States of AmericaS Steudel, R. 1975*$Properties of sulphur-sulphur bonds.14655-664:4Angewandte Chemie - International Edition in English~!BUilt'Qj+j6 j7j7j8`j8mj/jalowskir3 r3 r Urdkkalovul Ur [r)rXr,r,r,r,rr.r/.r.r.r11r15r1Pr1Qr1hr1ir1kr1lr1mr1nr1or1pr1qr1rr2r2r2r1jr1Vr49r4r4)r5r6r6r6r6r7r7'r76r7r8r8r0j r1n'rrinskyl0}laj2pg3Ddyrev5te2etg8RgGgedKddd+dXr,r,r,r,rr.r./r.r.r11r51rP1rQ1rh1ri1rk1rl1rm1rn1ro1rp1rq1rr1r2r2r2rj1rV1r94r4r)4r5rj0 rn1'rrinskyl}0lajp2gD3dyrevt5e2etgGgeKddd+dF?Torsion Angle Analysis of Glycolipid Order at Membrane SurfacesfBiophysical Journalu642i392-398Y Feb 3000.'Harfst, E. Johnstone, A.P. Nussey, S.S. 1992leANTIBODIES AUTOANTIBODIES BINDING CELLS CLEAVAGE CLONING HIGH-AFFINITY INTERACT PEPTIDES TSH RECEPTORExrCharacterization of the Extracellular Region of the Human Thyrotrophin Receptor Expressed as a Recombinant Protein("Journal of Molecular Endocrinology9n3227-236 Decn Feb S S S S S S!S!S!#S!0S!6S!BS!MS!fS!pS!S!S!S!S!S!S!S!S!S!S"S" S" S":S"JS"MS"RS"VS"aS"S"S"S"S"S"S#S#"S#6S#BS#CS#NS#TS#_S#lS#S#S#S#S#S#S$S$:S$CS$KS$QS$^S$\S$\Spes RNAiBackbone-driven assignment methods that utilize covalent connectivities have greatly facilitated spectral assignments of proteins. In nucleic acids, 1H-13C-31P correlations could play a similar role, and several related experiments (HCP) have recently been presented for backbone-driven sequential assignments in RNA. The three-dimensional extension of 1H-31P Het-Cor (P,H-COSY-H,C-HMQC) and Het-TOCSY (P,H-TOCSY-H,C-HMQC) experiments presented here complements HCP experiments as tools for sWongg oo o>i)i,i iii!i# i#i%-i%.i%/i%0i&i%1i+i+i,ci,xi/i1i2ni7oi i i\sirit igeit%2o4Hd8d>wwwmw,w&b'b4bbb b&bYbYbb$b%4b%3b%5b%9b%8b%6b%7b-Jbb&b2'b5'b5'b6w'b +buryrr%:m0c7c%;cockm*Hman8Qr Zruffs+s, s)s)s-Bs$s6Os7Ms7os7po*on55555555555***********kkkkkkppppppppppp`*1998*S9*9*T9*9)9*9)9)>9+9*9*9*9)9+*9*9)9)9*9+H9+K9+L9+M9+N9+O9+Q9+R9+S9+T9+U9+V9+W9)#9+X9+Z9+[9+\9+J9+]9+9+9* 9+q9+q9+q9+t9t+9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9+t9s'Qs+ss+ssiclesss(ssisssYs\ssssssoooo'o+o3o>obo)o&oTIONilit n np niak1993 G nStack1991 H Stack1991 W Stackhouse1987 X Stackhouse1988  Stadel19922 Y Stader1986 Z Stader1988 "v Stader1988 [ Stader1989 \ Stader1990 ]Stadtman1992N(SJEYS]S^S(S'_SSSS'BS)S#S`S(SS*SS +S :S(S(S S!-S!S!S!S*%S"@S)S*S)S(S"S(S*vS&S*S*hS&S)S$RS$RSR$S$RS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS$lS/NCbi/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d ( !$ ""%!" !$  Ġ  % %$不*!�  뻿 !, ￬ "$ ﷫ ! !$￯說(!$孨*!% $"꿿 "$ Davletovwes asony y.Ty3y4Ny7y7y7y7y7y7y7y7y7y7'yyCC i uih%h1gh2h2h3h4 h82h6zh7h7h)hoffi) iieB*hB'OB8A8A+XA+ZA+[A+\A+^A+_A+`A+aA+bA+cA+dA+eA+fA+gA+hA+iA+jA+kA+lA+oA+pA+qA+rA+wA+xA+yA+{A+|A+}A+~A+A+A+A+A+A+A+A+A+A+A+A+tA+YA+sA+sA ! ﺻ !믿* ( ((   ! (% "(  ? xfPOSTi)$e)e%e+^e+ke&e/e/e/e6pe6|e6e6e7,e8De8Ne8Te8he1eeapaaaa!'aoa)2a0aa5a6a7a7a7a8aa8ha8wa8a8a11a13a14a15a16a17a18a19a1:a1;a1<a1=a1?a1@a1Aa1Ba1Ca1Da1Ea1Fa1Ha1Ia1Ja1Ka1La1Ma1Na1Oa1Pa1Qa1Ra1Sa1Ta1Ua1Wa1Xa1Ya1Ya( 뿭 (J 翭( !0 ! 姈 *"!￭!! ! %꾿嵂* (!奧"(!%!%(ﻫ !$-B.5']5/b5+t5/5/5/5/5/5/5/5/5/5/5/5/5505x5t5u55-5/e5050505/50+50450950Q50R50U50M50O5-5/5.50\50_50i50j50w50x50z50{505050505050505050505050505050505 to host... Client message sent The Host closed the connection. Retrieving references 10 - 12... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 13 - 15... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 16 - 18... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 19 - 21... Sen @ ? > =D <T*Q ;V :v 3126@:Hendrix, J.C. Halverson, K.J. Jarrett, J.T. Lansbury, P.T. 1990JDOLIGOPEPTIDES ORGANIC-SOLVENTS OXIME POLYMER NETWORKS PROTEINS STATEA Novel Solvent System for Solid-Phase Synthesis of Protected Peptides - The Disaggregation of Resin-Bound Antiparallel Beta-Sheet"Journal of Organic Chemistry5515 4517-4518  20 Jul 31272,Hendrix, J.C. Halverson, K.J. Lansbury, P.T. 1992haCONDENSATION DEPOSITION DIMETHYL SULFIDE FRAGMENTS PEPTIDES SECONDARY STRUCTURE SEGMENT SYNTHESISEJCA Convergent Synthesis of the Amyloid Protein of Alzheimers Diseased.(Journal of the American Chemical Society 11420 7930-7931o 23 Sep Hengen, P.N. 19960*Eliminating ghost bands from plasmid preps$Trends in Biochemical Sciences21441-442 3129 Hengge-Aronis, R. Boos, W. 1986<5CONTROL ESCHERICHIA EXPORT PROTEIN SECA TRANSLATIONAL.*#The suppression of export of a class of periplasmic proteins of E. coli is caused by overprodn. of a C-terminal-truncated periplasmic enzyme GlpQ' (glycerophosphodiester phosphodiesterase). This truncated protein was not released into the periplasm but remained attached to the inner membrane and was accessible from the periplasm. The presence of GlpQ' in the membrane strongly reduced the appearance in the periplasm of some periplasmic proteins, including the maltose-binding protein (MBP), but did not affect outer membrane proteins, including the lambda receptors (LamB). The fate of MBP in comparison with the outer membrane protein LamB, was examd. Not only localization but also synthesis of MBP was impaired, indicating a coupling of translation and export. Synthesis and secretion of LamB were not affected. The possibility that this influence was exerted via the level of cAMP could be excluded. Synthesis of MBP with altered signal sequences was also reduced, demonstrating that export-defective MBP which ultimately remains in the cytoplasm abortively enters the export pathway. When GlpQ' was expressed in a secA51(Ts) strain, the inhibition of MBP synthesis caused by GlpQ' was dominant over the precursor accumulation usually caused by secA51(Ts) at 41.degree. Therefore, GlpQ' acts before or at the level of recognition by SecA. For LamB the usual secA51(Ts) phenotype was obsd. A mechanism is proposed by which GlpQ' blocks an yet unknown membrane protein, the function of which is to couple translation and export of a subclass of periplasmic proteins. 0021-9193`D>Translational control of exported proteins in Escherichia coli 167e2462-466&Konstanz D-7750, Fed. Rep. Ger.nJournal of Bacteriology 3130"Henikoff, S. Henikoff, J.G.i 1991|ALIGNMENT CDNA DISTANTLY RELATED PROTEINS ESCHERICHIA-COLI EXPRESSION HOMOLOGY MOTIFS NUCLEOTIDE-SEQUENCE PATTERNS REDUCTASEB;Automated Assembly of Protein Blocks for Database SearchingnNucleic Acids Research1923 6565-6572d 11 Dec 3132NGHenkel, T. Zabel, U. Vanzee, K. Muller, J.M. Fanning, E. Baeuerle, P.A. 1992z65-KD SUBUNIT ACTIVATION ANTIBODIES CELLS DNA ENHANCER BINDING PROTEIN HOMOLOGY RECEPTOR REL ONCOGENE TRANSCRIPTION FACTOR|Intramolecular Masking of the Nuclear Location Signal and Dimerization Domain in the Precursor for the p50 NF-kappaB Subunit Cell686 1121-1133 20 Mar 3131RLHenkel, T. Machleidt, T. Alkalay, I. Kronke, M. Benneriah, Y. Baeuerle, P.A. 1993{CELLS DNA-BINDING ENHANCER INHIBITOR INTERLEUKIN-1 INVITRO PHOSPHORYLATION PRECURSOR PROTEIN KINASE-C TUMOR NECROSIS FACTORtjcRapid Proteolysis of I-kappa-B-alpha Is Necessary for Activation of Transcription Factor NF-kappa-B3 Nature 365 6442182-1854 9 Sep 3133 Henley, J.M. 1993f_AMPA ANTI-PEPTIDE ANTIBODIES BINDING-SITES BRAIN CHANNELS GLUR KAINATE SPINAL CORD WESTERN BLOTAVOLocalization of AMPA Receptor Subunits in Rat CNS Using Anti-Peptide AntibodiesN Neuroreport4g3334-336 Mar #Peptide#s#s#s# s# s#0s#Vs#ms#s#s#s$s$s$%s$Ks$js$qs$ts${s$s$s$s$s%s%/s%0s%Hs%Ns%^s%\s%s%s%s%s%s%s%s&!s& s&"s&&s&*s&Ks&Js&Ps&Vs&bs&s&s&ws&s)1sss'Os'Js+gs+js+lss'Ps)2sLQANAloges ^srss5ssss 1s&,s&JsSssssfs sss*s;ssyss!s s"ss.sksjslssscss ;s"s#s&ssso oo)O O#O+yO6yO7oO7O7O89OOUS4 s s$| s6 s6` s6b s6w s6 s7 s7 s7 ssufuu u u u4W4a4%a44a4Ga4Ca4?a4<a41a4Na4Sa4Va4[a4_a4qa49a4xa4~a4a12a4)a4ta4a4a4a4a4a)aa1a)a(a4a4a)a4a4a$a%@a'Aa2Wa5?a5Ka5[a5da5ca5fa5sa5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a5a)two)5f)+f+Xf+_f%f+df'Jf+gfff)f+pf+|f+~f+f+fOf,f,f,f!;fNf'Sf+tf+Yf+sf0f0f0f0f0f1f0f=f+ f0f4f&f5f5f5f6f6 f6 f6 f6f6f6f6#f6%f6&f6-f61f63f64f65f67f68f6=f6Bf6Cf6Cf6Cf+~PRoteinsOO,O,O,O-O!;O'SO).O+O+YO+sO0O0O0O0O0O0O0O)/OO0O0O+ OzO0O4)c4c'Zc52c58c5c5c5c5c5c5c5c5c5c6c6c6c6 c6c6c6c6c6c6c6c6!c6&c6'c6)c6*c61c64c65c6=c6?c6?cistry 265o26 15432-15440 15 SepPley, U. Parham, P.  1993haClathrin: Its Role in Receptor-Mediated Vesicular Transport and Specialized Functions in Neurons28431-464 6181<6Critical Reviews in Biochemistry and Molecular Biology 6180,%Pley, H.W. Flaherty, K.M. McKay, D.B. 1994B;HAMMERHEAD RIBOZYME CRYSTALLOGRAPHY 3 DIMENSIONAL STRUCTURE :4Three-Dimensional Structure of a Hammerhead Ribozyme Nature 372~ 68-740; IVerfeldt ius ~wai)n{k+!k1kkurann,m3m5:m5{m0Nmatsuoto+nonn*TnnagaeAee(e-okasakiiXhita"ttae$e"e0Ve5e3\subo6Nthin X1zoyXy y1y!yyerzzzadyarrrd 0at+ t'ttootov umi%h!harayya /tani%su J o e{k!+k1kkurann,mN0matsuoto+nonnT*nnagaeAee(e-okasakiiXhita"ttae$e"eV0e5e X1zoyXy y1y!yyerzzzadyarrrd a0t +t'ttootov umi%h!harayya /tani%su J o e19923%3w33 3!3-h3h3 33-3#(333i3.333333l33q3.3K333-333#&3*330(30530=33303#3"3[303133-33$3333333U33333 *3!3$3536@3637 37X37c373&<3838393939393963333B33 3J33634333"M3+_33+3'Z3636373N33 2444!4&41454B4T4W4[4a4d4h4n4!4&41454B4T4W4[4a4d4h4n4. Albert19965i Albert2003T Alberti19931= Alberti20014y Alberti2002Q Alberts1989U Alberts1992)J Alberts1998V Albon19788 Alborn1991Albright19923k Alcazar-Roman1996*Alconada1993WAlconada1993"R Alcorn19929 Aldape1992  Aldape19949X Alder19908A Alder2003 RAlderman1985Y Aldhous1991 Aldrich1991  Alefsen1993Z Aleman1992/Aleshkov2000[ Alessi1993 1 Alessio2002 Alewood1990= Alewood1992= Alewood19920 Alewood1993\ Alexander1991 Alexander1992 Alexander1992 Alexander1992K Alexander1992` Alexander1992_ Alexander1992^ Alexander1992] Alexander1992  Alexander1993  Alexander1993  Alexander1993  Alexander1993a Alexander1993) Alexander1993, Alexander19985CAlexander Ross2002i4Alexander Ross2003c Alexandrescu1992d Alexandrescu1993 Alexandrescu1994f Alexandrescu1994e Alexandrescu1994g Alexandrescu1996* Alexandrescu1998*j Alexandrescu1998.4 Alexandrescu1999 Alexandrov1992 '> Alexandrov1993 h Alexandrov1993 3 Alexandrov2002i Alexis1992j Alfa1990v Alfano19849 Alfano1989tl Alfano1989 k Alfano1989  Alfano199002Alfarano20020 Ali1992 Ali1993o Ali19937 Alimov2000mAliverti1991 Alix1992n Alix1993v ? Alkalay1993) Allain19959) Allain1996 ) Allain1997 *. Allain1997 * Allain1998 +/ Allard1998 Allemann1993 Allen1990 Allen1990Z Allen1990J Allen19908 Allen1991 C Allen1992 Allen1992 D Allen1993 Allen19930H Allen1995/ Allen19990 Allen2000  Allerhand1979 Allert1993 9P Allert2004VAllewell1985Allewell1988Allewell1990 Allicotti19955g Allmann20038t Alloza2002k Allsop1992 T Allured1991. Alm1999. Alm19996 Alm1999/ Alm20002 Alm20002 Alm20007 Alm20002 Alm20014 Alm2002* Almeida1993! Almers1993" Almers1993 [ Almgren1991,2 Almlof1998. Almog1997^ Alnemri1991tAlobeidi1991 Alon1990 Alon1993z Alonso1989 Alonso1991 q Alonso1991 o Alonso1991 Alonso19911 Alonso1992d Alonso19921| Alonso1993  Alonso19933 Alonso1993 / Alonso200024r Alonso200305 Alonso20030! Alouf19913 Aloy2002ts Alper1992r Alper1992& Alpers1983 r Alpers1984 m Alpers1989 " Alpert199006: Alston199992: Alston2000< K Altamirano19939& Altamirano1997 6 Altamirano2000 Altenbach1992 Alter1992 Alter1993[ Althoff1992 Althoff1994t Althoff1994s Althoff19942Althorpe2002w, Altieri1995u Altman1990 Altman19911v Altman1991 $ Altman1992  Altman1992$ Altman1993  Altman19939w Altman1993 & Altman19979m Altmann1991n Altmann1992x Altmann1992x Altmann1992yAltschuh1992#Altschuh1993&+Altschuh199334Altschul19905Altschul1997z Alvares1990! Alvarez1977q Alvarez1979  Alvarez1991{ Alvarez1993 O Alvarez1993 : Alves1991! Alves1993 Alworth1992 Alzari1992 2 Alzhanova2001{ Amalric1990 Amalric1992 Amann1993% Amano1995 Amara1992 i Amaral1992  Amarneh1992| Amaya1991*T Ambler19989& Ambrosius1992 Ambrosius1993Amburgey1996,E Amemiya19984( Amemiya20025 Amemiya2003  America1993O Ames19900} Ames1992vP Ames19931 Ametani1993 Amherdt1991 Amherdt1993 Amherdt1993! Amherdt1993 Amherdt1993 Amherdt19931/ Amini2000~ Amir1988v Amir1992 Amirshapira1992 Amit1992v Amitay1992  Ammala1991 ! Amodeo19922 Amodeo1992  Amodeo1992 *M Amodeo1997 6u Amodeo1997+Y Amodeo19989# Amons1992> Amos1992 Ampe1993k Amrhein1994 Amsterchoder1992 Amsterdam1989QAmthauer1992 Amzel1992! Amzel1992X Amzel1993%` An19939/Z An19999_ An200506E Anand20015 Anand20028, Anand2003 Ananthanarayanan1991tAnantharamaiah1990?Anantharamaiah1990Anantharamaiah1992#VAnantharamaiah19939 Anborgh1993#Anderegg1994. Andereotti1998 Anders19900Andersen19919/Andersen19911Andersen19929TAndersen19929Andersen19929Andersen1992YAndersen1993Andersen1993 WAndersen1993 kAndersen1993 lAndersen19933Andersen19933Andersen1993Andersen1993)Andersen1995'QAndersen19966-Andersen19999-Andersen1999.Andersen1999-2]Andersen20012Andersen20022Anderson1973Anderson1975Anderson1976iAnderson1978Anderson1983Anderson19833Anderson19833Anderson19833GAnderson19833!ZAnderson19833 YAnderson19855![Anderson19866XAnderson1986Anderson1986Anderson1987Anderson1987Anderson1988 fAnderson1988%Anderson1989*Anderson1989Anderson1989$7Anderson1989Anderson1990Anderson1990 wAnderson1990Anderson1990Anderson1990Anderson1991>Anderson1991khAnderson1991`Anderson1991Anderson19911Anderson19919Anderson1991Anderson1991&Anderson1991Anderson1991Anderson1992Anderson1992Anderson1992Anderson1992Anderson1992Anderson19921 IAnderson1992Anderson1992Anderson1992Anderson19921"Anderson19922ZAnderson1992Anderson1993Anderson1993Anderson19939Anderson19939 WAnderson19939Anderson1993Anderson1993$ Anderson1993Anderson1993%Anderson1993^Anderson1994,Anderson1994)Anderson19959Anderson1996*cAnderson1997-Anderson1997*,Anderson1998.RAnderson19981Anderson19987vAnderson1998,Anderson1999B/SAnderson1999.3-Anderson2002w3Anderson20024[Anderson20024Anderson20037Anderson2003 Andersson1990 Andersson1992 Andersson1992 Andersson1993 Andersson1993 Andersson1994 Andersson1994% Andersson19969 Andersson2003zAnderton1991{Anderton1991 Anderton1991Anderton1992 Anderton1992|Anderton19933"Anderton1993/B Ando1973% Ando19929 Ando1993v5c Andrabi2003 Andrade1993 Andre1992% Andreadis1990 Andreazzoli19916% Andrec2003 Andree1993  Andreev1993" Andreeva197993Andreola2001w Andreotti19938B Andreotti2003 Andres1991 Andres1991  Andres19939 Andres1993 \ Andresson1992 Andreu19900dres1991 Andres1991 \ Andresson1992 Andreu19900 L@..=P0:07 4150:4Kuipers, O.P. Rollema, H.S. Devos, W.M. Siezen, R.J. 1993ANTIBIOTIC NISIN ANTIMICROBIAL ACTIVITY ASSIGNMENT CLONING EXPRESSION GENE IDENTIFICATION LACTOCOCCUS-LACTIS LEADER PEPTIDE MUTAGENESIS NISIN PREPEPTIDE PROTEINS SECRETION SUBTILINBiosynthesis and Secretion of a Precursor of Nisin-Z by Lactococcus-lactis, Directed by the Leader Peptide of the Homologous Lantibiotic Subtilin from Bacillus-subtilis FEBS Letters 330o1P 23-27 6 Seph60Kuivaniemi, H. Tromp,G. Chu, M.-L. Prockop, D.J. 1988[Structure of a full-length cDNA clone for the preproa2(I) chain of human type I procollagen 4 5 Biochemical Journal  252d633-640 JAHq,&Kuivaniemi, H. Tromp, G. Prockop, D.J. 1991VOMutations in collagen genes : causes of rare and some common diseases in humans FASEB Journal 5 2052-2060 JAHd 4152,&Kuliopulos, A. Shortle, D. Talalay, P. 1987Isolation and sequencing of the gene encoding delta 5-3-ketosteroid isomerase of Pseudomonas testosteroni: overexpression of the protein8424 8893-8897 DecVOProceedings of the National Academy of Sciences of the United States of AmericaS 4151:4Kuliopulos, A. Mildvan, A.S. Shortle, D. Talalay, P. 1989ngKinetic and ultraviolet spectroscopic studies of active-site mutants of delta 5-3-ketosteroid isomeraseO Biochemistry281I149-159P 10 JanXQKulkarni, S.K. Ashcroft, A.E. Carey, M. Masselos, D. Robinson, C.V. Radford, S.E. 1999HBA near-native state on the slow refolding pathway of hen lysozyme.Protein Science 8 35-44SJE JAH 4153:4Kumagai, H. Tajima, M. Ueno, Y. Yuhko, G.H. Ohba, M. 19912+BINDING FIBRONECTIN MELANOMA MOLECULES SITEdHBEffect of Cyclic RGD Peptide on Cell Adhesion and Tumor Metastasis:3Biochemical and Biophysical Research Communicationsc 177r1 74-82 31 May 4154>7Kumagai, I. Maenaka, K. Sunada, F. Takeda, S. Miura, K. 1993.'CONVERSION FOLDING DOMAINS NMR PROTEINSyleEffects of Subsite Alterations on Substrate-Binding Mode in the Active Site of Hen Egg-White Lysozymen& European Journal of Biochemistry 212m10151-156 15 Feb 4157.(Kumamoto, C.A. Oliver, D.B. Beckwith, J. 1984VPBINDING ESCHERICHIA GENE MALTOSE MUTATION PROTEIN SECA SECRETION SEQUENCE SIGNALSignal sequence mutants for an exported protein, maltose-binding protein, prevent the blockage of synthesis of this protein in a secA mutant of Escherichia coli.n 0028-0836ovpSignal sequence mutations disrupt feedback between secretion of an exported protein and its synthesis in E. coli 308o 5962863-864Boston, MA 02115, USAn Nature"Kumamoto, C.A. Gannon, P.M.. 1988pjEffects of Escherichia Coli SecB Mutations on Pre-Maltose Binding Protein Conformation and Export Kinetics 263a 11554-11558h&Journal of Biological ChemistryP 4155Kumamoto, C.A. 1991yCOMPETENT STATE EXPORT GENE-PRODUCTS GROEL INVITRO MALTOSE BINDING PROTEIN MUTATIONS PRO-OMPA SECB PROTEIN TRIGGER FACTOR`YMolecular Chaperones and Protein Translocation Across the Escherichia-Coli Inner MembraneeMolecular Microbiology51 19-22  Jan 4156"Kumamoto, C.A. Francetic, O. 19934.5 S-RNA EXPORT MACHINERY INNER MEMBRANE MATURE LAMB PROTEIN MOLECULAR CHAPERONES MUTATIONS SECB SECRETED PROTEINS SIGNAL RECOGNITION PARTICLE TRANSLOCATIONf`Highly Selective Binding of Nascent Polypeptides by an Escherichia-Coli Chaperone Protein InvivoJournal of Bacteriology 1758M 2184-2188M Apr1997Negatively Charged Amino Acid Residues Play an Active Role in Orienting the Sec-independent Pf3 Coat Protein in the Escherichia coli Inner Membrane EMBO Journal169i 2197-2204 3872*#Kieffer, B. Koehl, P. Lefevre, J.F. 1992d^ANTIBODY DYNAMICS HEMAGGLUTININ INFLUENZA-VIRUS MODES NMR PEPTIDE PROTEIN DYNAMICS SIMULATIONSNHModelling the Dynamics of an Antigenic Peptide Using NMR Relaxation Data Biochimie 74 9-10815-824oSep-Octe2Junner6branicetichgenshivichka&s8wt3 'ssieut xxx -xx*]x$x1 x7xx-xCxv)&i5i5i6i7i7i7i8i6x ification6}ed y ntte6ulnvenile$"Qx$v*vadix4 xtamembraneW pnuclearposed6!ition6 s@ sy)ZVW).K9'b9/b9\b8G'backK K i#ashivichka&s3 'ssieut xxx -xx*]x$x1 x7xx-xCxv)&i5i5i6i7i7i7i6x ification6}ed y ntte6ulnvenile$"Qx$v*vadix4 xtamembraneW pnuclearposed6!ition6 s@ sy)ZVW).K K i#a#aa&198#0 0$0)10001?1v11111111R1Q1P1g1 1 1 1 1 1 1 1 1 1 i1 1 11#1111&1111 1F1Y111111111 E1 l1"|1%t11!1215N11 1=1J1I20$0)10001?1v11111111R1Q1P1g1 1 1 1 1 1 1 1 1 1 i1 1 11#11111&1111 1F1Y111111111 E1 l1!1"|1%t11 1=1J1I2 PRoteOlysis t t t t t t t$ t' tA t t  ta t t  t! t# t$b t$ t$ t tx t#z t# t$ t+Y t6 t6 t6 t6 t6 t6 t6 t7 t7 t7$ t7p t7r t7 t7 t88 t8g tticU H9 HG H H H~ H H6 H  H  H H H H H H H H HL H' H; HG HJ Hq H H H' H HJ H H%  H% H&$ H&& H&4 H H.  H06 H $ t tx t#z t# t$ tticU H9 HG H H H H~ H H6 H  H  H H H H H H H H HL H' H; HG HJ Hq H H H' H HJ H H%  H% H&$ Ho H H6 capacities# Oo O  O Os O3ory\ yly#IIII I II&IINI<I>IBI#I I!I#6I%I%I]I|II I l,ll`lllllQlllllBlCl#ll!,l#l$l%ll%Dlllllzl!ol'Ql0l68l6ml6l7al7l8l)ldi-Yi-Zi1i1n0n1n1n5Bn6n0nni6i7i9jellix+ieauxeaux,G+2+2,+2,.2,52)2*22a2*2+02*2,A2,B2+2,E2,F2,O2,P2,S2 2*2)2,e2(2,l2+2+2(2,u2,w2,|2,2*w2,2,2,2,2,2,2,2,2,2,2,2,2,2,2*2+2- 2- 2*0222-2X2X2X2X2X2X2X2Ray$ee e e e e e e e e Se ce "e)e&e e \e re we e e ezeeeee eeeeeeee?eBeeeDeZe`eepeweeeeLeeeeee'ee.e\ewee)Gee2e,Journal+u,u,u,u,u,u,u,u,u,u,u,u-u-uu)Su)Ru-&u*u'uuu'uuFu+u+u uXu Muu,u,u)u!9u(uuUu,u#uuuAunuqupuu u,!uuupuquuuu(u)u+u+u+u+uAviandldddrd 1d"d"d#Qd8dinl l l4t8ht\tyl7lygelognon?l-k,k!klae3eeee e deeeeae*Fest t" tq/,7 +st tal5y'v5'n nio4:oide-e5e6xe7$e7e8a8?a8ga8ya8Tanceeedi6i ing"u6?s8ss)1s7!s8s&s7u!ustin"ril#ons wW+w68a6are y r&r'Sr6r6^r6ar6r7r8Er8r)&ryu6 ueous-xei$lsenizi Qi)i65s6;i6]i#ial!=l1l lRl7lBllarys l#l#lBllarys l#l#s*+ 6N4( ( 3912ZSKim, K.S. Tao, F. Fuchs, J. Danishefsky, A.T. Housset, D. Wlodawer, A. Woodward, C. 1993AREA BPTI COLD DENATURATION CRYSTAL-STRUCTURE EXCHANGE HYDROGEN-EXCHANGE KINETICS MYOGLOBIN PARAMETERS PROTEIN FOLDING PROTEINS SOLUTES THERMODYNAMICS THERMOSTABILITY WATERtnCrevice-Forming Mutants of Bovine Pancreatic Trypsin Inhibitor - Stability Changes and New Hydrophobic SurfaceProtein Science2i4588-596 Apri 3911*$Kim, K.S. Fuchs, J.A. Woodward, C.K. 1993ALZHEIMERS-DISEASE AMIDE PROTON-EXCHANGE CRYSTAL-STRUCTURE CYTOCHROME-C EGG-WHITE ISOTOPE EXCHANGE NMR NUCLEAR MAGNETIC-RESONANCE PANCREATIC TRYPSIN-INHIBITOR PEPTIDE^WHydrogen Exchange Identifies Native-State Motional Domains Important in Protein FoldingA Biochemistry3237 9600-9608a 21 Sep SJEI 3900$Kim, D. Lee, Y.J. Corry, P.M.h 1993CELLS CHAIN BINDING-PROTEIN CLATHRIN COATS COATED VESICLES DISSOCIATION HSP70 PROTEIN AGGREGATION PURIFICATION RAT RHODANESE SHOCK PROTEIN STRESS PROTEINS TURBIDIMETRIC ASSAY UNCOATING ATPASEc|uEmployment of a Turbidimetric Assay System to Study the Biochemical Role of HSP70 in Heat-Induced Protein Aggregationr Journal of Thermal Biology183165-175 Jun8Kim, C.W.A. Berg, J.M. 1993LThermodynamic b-sheet propensities measured using a zinc-finger host peptide    Nature 362 6417267-270 18 Mar 3898~DEPENDENT STRUCTURE GLOBULAR-PROTEINS HELIX-FORMING TENDENCIES OCCURRING AMINO-ACIDS PREFERENCES SECONDARY STRUCTURE STABILITY 393060Kim, Y.H. Higuchi, W.I. Herron, J.N. Abraham, W. 1993^X1,6-DIPHENYL-1, 3,5-HEXATRIENE FLUORESCENCE ENERGY-TRANSFER ENHANCEMENT FACTOR FATTY-ACIDS FLUIDITY FLUORESCENCE ANISOTROPY FLUORESCENCE LIFETIME INTERDIGITATED GEL PHASE LABELED PHOSPHATIDYLCHOLINE LECITHIN BIMOLECULAR LEAFLETS PLASMA-MEMBRANE PROBES SHORT CHAIN N-ALKANOL STRATUM-CORNEUM LIPID LIPOSOME STRUCTURAL ORDER TEMPERATURE-DEPENDENCEFluorescence Anisotropy Studies on the Interaction of the Short Chain N-Alkanols with Stratum Corneum Lipid Liposomes (SCLL) and Distearoylphosphatidylcholine (DSPC)/Distearoylphosphatidic Acid (DSPA) Liposomes$Biochimica et Biophysica ActaP 11481139-151 14 May 3929LEKim, S.K. Nielsen, P.E. Egholm, M. Buchardt, O. Berg, R.H. Norden, B. 1993`ZANTISENSE CLEAVAGE CURVES DNA HELIX FORMATION POLYNUCLEOTIDES RECOGNITION SEQUENCE THYMINERight-Handed Triplex Formed Between Peptide Nucleic Acid PNA-T(8) and Poly(dA) Shown by Linear and Circular Dichroism Spectroscopy.(Journal of the American Chemical Society 11515 6477-64815 28 Jul("Kim, Y.J. Rajapandi, T. Oliver, D. 1994dSecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state:A Cell78845-853 SSG  3928*$Kim, S. Willison, K.R. Horwich, A.L. 19944-CHAPERONINS ATPASE POLYPEPTIDE BINDING DOMAINpreviewsDleCytosolic Chaperonin Subunits Have a Conserved ATPase Domain but Diverged Polypeptide-Binding Domains$Trends in Biochemical Sciences19543-548*#Kim, S.J. Robinson, D. Robinson, C.  1996An Arabidopsis thaliana cDNA encoding PS II-X, a 4.1 kDa component of photosystem II: A bipartite presequence mediates SecA/Delta pH-independent targeting into thylakoids FEBS Letters 390 2175-178("Kim, K. Cistola, D. P. Frieden, C. 1996`ZIntestinal fatty acid-binding protein: the structure and stability of a helix-less variant Biochemistry35 7553-7558L ifabp folding  SJE("Kim, K. Ramanathan, R. Frieden, C. 1997Intestinal fatty acid binding protein: A specific residue in one turn appears to stabilize the native structure and be responsible for slow refoldingFProtein Sciencer6364-372SJE KSR0)Kim, H.S. Hartgerink, J.D. Ghadiri, M. R.a 1997LEOriented self-assembly of cyclic peptide nanotubes in lipid membranesr.(Journal of the American Chemical Society 120 4417-4424 Oct 8XQPolarized attenuated total reflectance (ATR), grazing angle reflection- absorption, and transmission Fourier transform infrared (FT-IR) spectroscopy methods have been used to investigate the orientation of peptide nantoubes in the functionally relevant environment of ordered phospholipid multibilayers. Eight-residue cyclic peptides of alternative D-and L-amino acids which self-assemble to form open-ended tubular structures have been shown previously to funciton as transmembrane channels for ion transport. Although the tubular structure of the pepetide assembly has been established in the pure solid state, this study present the first detailed biophysical invesitgation of the peptide nantoubes iwthin the context of the lipid film to afford a quantitative estimate of their angle fo orientation relative to the lipid bilayer. We find by ATP IR that in accordance with the previous structure-funciton model hypothesis for a transport-comeptent channel, teh central axis of nanotubes composed of cyclo[(L-Trp-D-Leu)3-L-Gln-D-Leu] is aligned paralle to the dimyristoyl phsophatidylcholine (DMPC) hydrocarbon chains at aproximately seven degrees form teh axis normal to the bilayer plane. This upright orinetation for th eDMPC/;petpdie film is also qualitatively supported by grazing angle and transmission FT-IR data. By cotnrast, FT-IR studies of two- and three-dimensionally ordered peptides Langmuir-Blodgett films and microcrystals, respectively, show that hte peptide tubes lie parallel to the substrate surface in teh absence of a hydrophobic supportive enivronment. These studies support a transport-competent, membrane-spanning orienation of the peptide nanotubes in the lipid bilayers. Furthermore, they indicate that the orientation fo the tubes cna be controlled by a supporting environment, implicaiton biological and nanotechnological applications.oKim, S Baum, J 1998`ZElectrostatic interactions in the acid denaturation of alpha-lactalbumin determined by NMRProtein Scienced7t 1930-1938lD>chemical exchange ionizable groups NMR pH titration pKa valuesKSR, in filecabinet  Kim, D.E. Gu, H. Baker, D. 1998leThe sequences of small proteins are not extensively optimized for rapid folding by natural selection.VOProceedings of the National Academy of Sciences of the United States of America95 4982-4986d SJE Kagami1992% Kagamiyama1993  Kagan1992 - Kagechika19936Kagemoto1989Kagemoto1990 Kagi19900 Kagi19900M Kagi19929JKagiwada19922KKagiwada19933v Kaguni1991 Z Kaguni1993Y Kaguni1993  Kahana1992  Kahn19911 Kahn1991v Kahn19911 Kahn19919 Kahn1992v Kahn1992v Kahn19922% Kahn1992 Kahn1992'0 Kahn19939 Kahn199331 Kahn2002 Kahne1993IKaibuchi1993 Kail1991v"Kainosho1991gKainosho19933Kainosho19939*Kainosho1997 Kairi19904 Kaiser1970 Kaiser19733 Kaiser1984 /; Kaiser19844[ Kaiser1990 Kaiser19922Q Kaiser19939* Kaiser1998  Kajava1991 L Kaji19929 Kaji1993v Kaji1993v8Kajimoto20022 Kajtar19900 Kajtar19900 Kajtar19911 Kajtar19922 Kajtar19939 Kajtar19933!1 Kajtar19933 Kakalis1992 Kakeda1991 Kakitani19844Kakitani1985Kakitani1985Kakitani19855@Kakiuchi1993%N Kakoschke1993.Kakouras19999 Kalbach1993 Kalbacher1991 Kalbacher1992 Kalbacher19934 Kalback2002 Kalbitzer1992 Kalbitzer1992 Kalbitzer19934< Kalbitzer2002$Kaldenbergstasch1993 Kaldi19934 Kalia1993' Kalies19929 Kalies1996 )# Kalies199811u Kalies200000 Kalinke2001-{ Kalinowski1998$Kaljuste1993 Kalk19933% Kalland1996 Kallen19729 C Kallen19921g Kallenbach1980 h Kallenbach1984  Kallenbach1986  Kallenbach1989 W Kallenbach1990  Kallenbach1990 Y Kallenbach1991 X Kallenbach1991 r Kallenbach1991 [ Kallenbach1992 Z Kallenbach1992  Kallenbach1993  Kallenbach1993 \ Kallenbach1993  Kallenbach1994&r Kallenbach1994 1 Kallenbach2002+Kallunki1998$0- Kalnin1995 Kaloss1993 Kalousek1992Kalousek1993-`Kalousek19933/ Kaltashov1999-P Kaltashov20007 Kaltashov2002 Kaluza19939, Kaluza199490Kalverda20003VKalverda200224+Kalverda2002 Kam1991+ Kamada1998 6 Kamada2003l4(Kamagata20025Kamagata2003 #Kamakura199283 Kamal2003@Kamatani1993/Kamatari2000!8 Kamath1993, Kamath-Loeb19956 Kamath-Loeb1995$ Kamathloeb1992 Kamatkar1993( Kamawal1997 Kamaya19922 Kamaya19929 Kambehonjoh1992{ Kamber1972 " Kamber19933* Kamen20023+ Kamen2002Kametani1992/ Kami2000/Kamikubo2000!  Kaminogawa1993  Kaminoh199297Kaminski2001lKaminsky1992AKamitani1992Kamitani1992$tKamitsos19929F Kamiya19909 Kamiya1992$ Kamiya19939Kamketar1993Kammerer1996*jKammerer199892 Kammermeier2000 Kammesheidt1992*Kammlott1998! Kamogashira1992  Kamoshita1979 Kampe1990 Kamphuis19929"?Kamphuis199332Kampinga200001eKampinga20011Kamtekar19932 Kana2000p Kanagy19911x Kanai1992 Kanai1992" Kanai1993"Kanamori1993%* Kanaoka1991 Kanaya19858 Kanaya19909 Kanaya19900 Kanaya1990  Kanaya1990  Kanaya1991 Kanaya1992 Kanaya19922 Kanaya19939 Kanaya19939 Kanaya1993 , Kanaya19959, Kanaya19979) Kanaya1998u/ Kanaya2000% Kanda1991/ Kandori1999 Kandror1994- Kane1996;Kanehisa1993' Kaneko19919! Kaneko199292 Kaneko199992 Kaneko2000 0 Kaneko2001 2 Kanelakis20002 Kanelakis20002 Kanelakis20012 Kanelakis20014 Kanelis2001Kanemaru19925Kanemori2002 Kang1990 Kang1990v Kang1991vL Kang19939" Kang19931$~ Kang19939 T Kang19939 Kang1993v Kang1996vR Kang199692 Kang2000, Kanner199393 Kanno20023 Kano199391e Kanon2001 Kanost1988 ' Kansal19900, Kanter19989 Kantor1977 . Kao1998-; Kao19995 Kao2003 X Kapadia19926r Kapanidis2002 Kaper1992Kapiloff19929U Kapitkovsky1990  Kapitonov1991 Kaplan1991919922Q Kaiser19939* Kaiser1998  Kajava1991 L Kaji19929 Kaji1993v Kaji1993v Kajtar19900 Kajtar19900 Kajtar19911 Kajtar19922 Kajtar19939 Kajtar19933!1 Kajtar19933 Kakalis1992 Kakeda1991 Kakitani19844Kakitani1985Kakitani1985Kakitani19855@Kakiuchi1993%N Kakoschke1993.Kakouras19999 Kalbach1993 Kalbacher1991 Kalbacher1992 Kalbacher1993 Kalbitzer1992 Kalbitzer1992 Kalbitzer1993$Kaldenbergstasch1993 Kaldi1993' Kalies19929 Kalies1996 )# Kalies199810 Kalinke2001-{ Kalinowski1998$Kaljuste1993 Kalk19933% Kalland1996 Kallen19729 C Kallen19921g Kallenbach1980 h Kallenbach1984  Kallenbach1986  Kallenbach1989 W Kallenbach1990  Kallenbach1990 Y Kallenbach1991 X Kallenbach1991 r Kallenbach1991 [ Kallenbach1992 Z Kallenbach1992  Kallenbach1993  Kallenbach1993 \ Kallenbach1993  Kallenbach1994&r Kallenbach1994 +Kallunki1998$0- Kalnin1995 Kaloss1993 Kalousek1992Kalousek1993-`Kalousek19933/ Kaltashov1999-P Kaltashov2000 Kaluza19939, Kaluza199490Kalverda2000 Kam1991+ Kamada1998 #Kamakura1992@Kamatani1993/Kamatari2000!, Kamath-Loeb1995$ Kamathloeb1992 Kamatkar1993( Kamawal1997 Kamaya19922 Kamaya19929 Kambehonjoh1992{ Kamber1972 " Kamber1993Kametani1992/ Kami2000/Kamikubo2000!  Kaminogawa1993  Kaminoh1992Kaminsky1992AKamitani1992Kamitani1992$tKamitsos19929F Kamiya19909 Kamiya1992$ Kamiya19939Kamketar1993Kammerer1996*jKammerer19989 Kammesheidt1992*Kammlott1998! Kamogashira1992  Kamoshita1979 Kampe1990 Kamphuis19929"?Kamphuis19933Kamtekar1993 Kanagy19911x Kanai1992 Kanai1992" Kanai1993"Kanamori1993%* Kanaoka1991 Kanaya19858 Kanaya19909 Kanaya19900 Kanaya1990  Kanaya1990  Kanaya1991 Kanaya1992 Kanaya19922 Kanaya19939 Kanaya19939 Kanaya1993 , Kanaya19959, Kanaya19979) Kanaya1998u/ Kanaya2000% Kanda1991/ Kandori1999 Kandror1994- Kane1996;Kanehisa1993' Kaneko19919! Kaneko199290 Kaneko2001 Kanemaru1992 Kang1990 Kang1990v Kang1991vL Kang19939" Kang19931$~ Kang19939 T Kang19939 Kang1993v Kang1996vR Kang19969 Kanner199393 Kano199391e Kanon2001 Kanost1988 ' Kansal19900, Kanter19989 Kantor1977 . Kao1998-; Kao1999 X Kapadia1992 Kaper1992Kapiloff19929U Kapitkovsky1990  Kapitonov1991 Kaplan1991919919\~0: 36472,Jones, T.A. Blaug, G. Hansen, M. 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Aug 412482Kropshofer, H. Bohlinger, I. Max, H. Kalbacher, H. 1991BINDING-SITE CELL RECOGNITION EPITOPES HISTOCOMPATIBILITY COMPLEX ANTIGENS INFLUENZA NUCLEOPROTEIN INVARIANT CHAIN MOLECULES RESTRICTED LYMPHOCYTES-T SPECIFICITY SYNTHETIC PEPTIDES B Hilbich, C. Monning, U. Grund, C. Masters, C.L. Beyreuther, K. 1993XQALZHEIMERS-DISEASE BETA-A4 PEPTIDES BINDING CONFORMATION CONGO RED IDENTIFICATION~xAmyloid-Like Properties of Peptides Flanking the Epitope of Amyloid Precursor Protein-Specific Monoclonal Antibody-22C11&Journal of Biological Chemistry 26835 26571-26577 15 Dec 3180<5Hildebrandt, J.D. Day, R. Farnsworth, C.L. Feig, L.A. 1991ADENYLATE-CYCLASE BINDING-PROTEIN G-PROTEINS GTP HYDROLYSIS GUANINE NUCLEOTIDES HA-RAS MUTATION MOLECULAR-CLONING NIH 3T3 CELLS REGULATORY COMPONENT SIGNAL TRANSDUCTIONd^A Mutation in the Putative Mg-2+-Binding Site of GS-alpha Prevents Its Activation by Receptors$Molecular and Cellular Biology1110 4830-4838 OctHill, R.L. 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Kinetic investigations Biochemistry282691-699 24 Jan 1160,&Chen, W.J. Goldstein, J.L. Brown, M.S. 1990NPXY, a Sequence Often Found in Cytoplasmic Tails, Is Required for Coated Pit-Mediated Internalization of the Low Density Lipoprotein Receptor&Journal of Biological Chemistry 265 3116-3123 1157<5Chen, S.Y. Cheng, K.H. Vandermeer, B.W. Beechem, J.M. 1990CA-ATPASE VESICLES DEPOLARIZATION ENERGY-TRANSFER HII PHASE INVERTED PHASES L-ALPHA LIQUID-CRYSTALS MEMBRANE-FUSION PHOSPHATIDYLCHOLINE VESICLES PHOSPHATIDYLETHANOLAMINEovoEffects of Lateral Diffusion on the Fluorescence Anisotropy in Hexagonal Lipid Phases .2. An Experimental StudyoBiophysical Journal586  1527-1537 Dec 1155Chen, S.Y. 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Peterson, P.A. 1992ANTIGEN ANTIGEN PRESENTATION BETA 2 MICROGLOBULIN BINDING CYTOTOXIC T-CELL FUNCTIONAL CDNA HEAVY-CHAIN INTRACELLULAR-TRANSPORT INVITRO PEPTIDE BINDING PROTEIN RECOGNITION RETROVIRAL SHUTTLE VECTOR SEQUENCESEmpty and Peptide-Containing Conformers of Class-I Major Histocompatibility Complex Molecules Expressed in Drosophila-Melanogaster Cells8924 12117-12121 15 DecVOProceedings of the National Academy of Sciences of the United States of AmericaR 3495 Jackson, M. Mantsch, H.H.0 1992PIHalogenated alcohols as solvents for proteins: FTIR spectroscopic studies$Biochimica et Biophysica ActaN 1118139-143s 3491LFJackson, A. Friedman, S. Zhan, X. Engleka, K.A. Forough, R. Maciag, T. 1992|BINDING ENDOTHELIAL-CELLS EXPRESSION FACTOR-I HUMAN HSP70 OUTER SEGMENTS SEQUENCE SHEAR-STRESS STRESS PROTEINS TRANSLOCATIONVOHeat Shock Induces the Release of Fibroblast Growth Factor-1 from NIH-3T3 Cellso8922 10691-10695 15 NovVOProceedings of the National Academy of Sciences of the United States of AmericaRjcJackson, G.S. Staniforth, R.A. Halsall, D.J. Atkinson, T. Holbrook, J.J. Clarke, A.R. Burston, S.G. 1993Binding and hydrolysis of nucleotides in the chaperone catalytic cycle: implications for the mechanism of assisted protein folding.  Biochemistry32 2554-2563 ,&Jackson, S.E. Elmasry, N. Fersht, A.R. 1993Structure of the hydrophobic core in the transition state for folding of Chymotrypsin Inhibitor-2 - A critical test of the protein engineering method of analysis" Biochemistry3242 11270-11278d 26 Oct 3500"BARNASE ENZYME INTERMEDIATE  JAHd 3493jcJackson, G.S. Staniforth, R.A. Halsall, D.J. Atkinson, T. Holbrook, J.J. Clarke, A.R. Burston, S.G. 1993ATP HYDROLYSIS ESCHERICHIA-COLI GROE HEAT-SHOCK HSP60 LACTATE-DEHYDROGENASE PURIFICATION RHODANESE RIBULOSE BISPHOSPHATE CARBOXYLASE STATEBinding and Hydrolysis of Nucleotides in the Chaperonin Catalytic Cycle - Implications for the Mechanism of Assisted Protein Folding Biochemistry3210 2554-25630 16 Mar\Maykcxcccccccccccc3cKcNcYcsccccccccccc c c &c Ac ic xc c c c c c!c!c!Ac!Nc!Xc!c!c!c!c" c"c"#c"<c"=c"Kc"c"c"c"c"c"c"c"c"cVItsJJJJJJ9JOJeJfJJ)9JJJ JJ$JKJkJJJJJJJ3J7J*|J)JJJ ?J J J J J!4J!6J!GJ!RJ!TJ!cJ!J!J!J"J"J"TJ"dJ"eJ"J"J)J)NJ)J#J#J#J$J$J$+J+$J$+J%6FOr%MC%aC%{C%|C%C%C'WC%C%C%C%C%C%C%C%C%C%C%C%C%C& C& C&C&C+C&C(C&+C&?C&>C&PC&VC&aC&bC&cC&C&gC&C&rC&xC&C&C&C&C&C'C+MC+\C+JCC'KCC+eC'JC*C*C*C*C*C*C*C*C*C >{ Z k sy >{ ZPk syfix FieldsE >{ Zpk0 sy >{ Zk0 sy ;~ ;| ; >{ ;(nica ZkP sy >{HH ; Zk0 sy >{ Z@k sy >{ Zpk sy >{ Zk0 sy >{ Zk0 sy ; ;H ; >{ ;} Z kP sy ;`10942822934 #92$732)02& 5&N931194421"507860817569 968$AcidnZDvances'lphaiminoisobutyricNdeerson&Pre Ussembly$vianey Bacteriologyn%essalleIndings\ Ochemistryxphysica"oyd y# C4ation#HainsemistryleavaGEompared nsequences3rowdedaD3 ehydrOgenasei! terMINAtion*imyristoylphosphatidylL"&NAKYnamics$}EFfecto L Ndoprotease#rYTHROBLASTOSIS xaminationA F IBROBLASTSooldingrrAmeworkG EneticHA onadOTROPinH~ eadgroups1x'Biology1~'u1'u1'u1'u1'u1'u1'u1'u1'u1'u1'u1'u1'u1'u1'u2w'u2x'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u2'u3'u3 'u3'u3'u3'u3'u3'u3#'u3&'u3'u2'u3'u3'u3'u4CQUery4?s4As4@s4>s4<s41s4Is4Us4Ms4Ns4Os4Ps4Qs4Rs4Ss4Ts4Vs4Ws4]s4\s4[s4Zs4Ys4Xs4gs4fs4es4ds4cs4bs4as4`s4_s4^s4ns4ms4ls4ks4js4is49s12s4)s4s4s4s4s4s4s4s4s4s4s4s4s4s4s4s4s1s1s1s4i' university4p' k4q' k4r' k4x' k4' k4' k4' k4' k4z' k4{' k4|' k4~' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4)' k4s' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4' k4:' k5D' k5E' k5G' k5H' k5K' k5J' k5M' k5L' k5P' k5O' k5T' k5Y' k5X' k5V' k5]' k5[' k5c' k5`' k5l' k5k' k5i' k5h' k5h' kh5' k>Boydd"P!P%P&P'Cllxe'YeDeeeee"`e"ae#e0e4en46er l2'l7'l(lan e'e)esen(hmerpN^NNNNN6g'c7'I8y'I6QI6N6QNNTT T T TTT T T!QT-T. T.!T\T T TKTT T!TZT. T.!T&TIrrrr5XNlm5WS5VS5]S5\S5[S5ZS5^S5dS5cS5bS5aS5`S5_S5lS5kS5jS5iS5hS5gS5fS5mS5qS5pS5oS5sS5rS5zS5yS5xS5wS5vS5uS5tS5S5S5S5S5S5S5~S5}S5|S5{S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S5S6 H6 a6a6a6a6!a6(a6*a6+a6-a64a6Na6Wa6da6ea6fa6ga6ha6ia6ma6ra6ya6}a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a6a7a7a7 a7a7a7 a7'a7.a7:a7=a7Ca7Ma7Ra7Ta7Wa7Za7\a7]a7aa7ga7ia7ja+%Journal+u2u4u4u4u4u4uUu(uu4u4u4uu&u1uu4u4u4u4u u/yu4u)u'Zu% u%ju4u%Du4u4u2Wu5u5u(u55u56u57u5>u5?u5Au5Bu5u5u5u5u5u5u5u5u5u5u5u6 u6u6u6u6u6u6>u6Du7M7777777777777888 8,8888 68$8+8-8.8283858:8=8?8A8D8F8K8L8N8P8R8V8W8]8_48d8j8l8p8r8s8w8z8}8~8888888tml20207052 SJEe*$Li, L. Mirny, L.A. Shakhnovich, E.L. 2000d^Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus Nature Structural Biology7336-342Guna-for review Li, J. Zhang, S. Wang, C.\ 2001~xEffects of macromolecular crowding on the refolding of glucose-6-phosphate dehydrogenase and protein disulfide isomerase&Journal of Biological Chemistry 276D37 34396-34401 JAHT Haussler1984 S Hauw19922' Havekes1993W Havel1989 Havel1991  Havel1991  Havel1991# Havel1992z Havel1992 Havel1993Havelund19933/ Haverkamp20008o Haverkamp20022 Havert200107q Havlin2001x Hawe19933 Hawes1992  Hawes1993 Hawiger1992 Hawkes19819 Hawkins1989  Hawkins1991 Hawkins1993& Hawkins1997- Hawkins1998  Hawrot19909 Hawrot1993 /{ Hay19995bHayaishi2003Hayamizu1993 Hayano19909!R Hayano19919  Hayano1993- Hayano19996G Hayano2000$& Hayashi1988& Hayashi1991 Hayashi1992% Hayashi1992* Hayashi1992 Hayashi1993  Hayashi1993 n Hayashi1993 Hayashi1993 Hayashi1993 Hayashi1993 Hayashi1993/8 Hayashi19993? 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He1999@9^ He20030% Head19919 Head199399j Head20052  Headgordon1991  Headgordon1992  Headgordon1993 $ Heald1990g Heald19910 Healy2000 } Heard1996  Heath1993 Hebert199390C Hebert199492; Hebert20018@ Hebert20033 Hecht1983  Hecht1983 Hecht1983  Hecht1984  Hecht1985  Hecht1985  Hecht1986  Hecht1990  Hecht1992B Hecht1992 Hecht1993  Hecht1993 Hecht1993 Hecht1993$ Hecht1995* Hecht1995$ Hecht1996( Hecht1997. Hecht1999/ Hecht20003 Hecht20023 Hecht20026 Hecht2003/ Heck20008o Heck20020' Hecker1992 Hecker1992$ Hecker1992* Hedge1998f Hedgepeth1992QHedgpeth1980Hedgpeth19811 Hedleywhyte1992% Hedlund1981" Hedlund1992% Hedlund1996. Hedstrom1998 Heegaard19930Heegaard2001i Heemels1990  Heemels1993 Heemeyer1994  Heemskerk1993  Heerze1992 5 Heerze199398 Heffelfinger20038 Hefford2002  Hegde19938 Hegde1994)! 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Helms1993- Helms1999  Hemingway1993 Hemker19933& Hemler1991 l Hemmi1992Hemminga19911Hemminga19911 NHemminga1991# Hemminga19919 *Hemminga1992Hemminga1992Hemminga19922Hemminga1992%)Hemminga19939Hemminga1993 +Hemmings1992 , Hemmingsen1988  Hemmingsen1990 n Hemmingsen1992 m Hemmingsen1992 - Hemmingsen1992  Hemmingsen1993  Hemmingsen1993 %^ Hemmingsen1993 .Hemphill1992]Hemphill19931 / Hemsley19894 Henault2002,v Henckel1997] Hendershot1990  Hendershot1993 8 Hendershot1993* Hendershot1998 2 Hendershot19993 Hendershot20024s Hendershot2002 0 Henderson1992 1 Henderson1993 Henderson1994-q Henderson1996*T Henderson19986 Henderson2002. Hendle1997Hendrick1990 Hendrick1990Hendrick1991 2Hendrick1991 6Hendrick1993 7Hendrick1993 8Hendrick1995*Hendrick1997-Hendrick1999* Hendrickson1991$T Hendrickson1992&} Hendrickson1996-, Hendrickson1996* Hendrickson1998.> Hendrickson19982 Hendrickson20023jHendriks2000 Hendrix1973 9 Hendrix1979Helenius1993 % Helferich1986 Helfman1992 Helfman1992 OHelfrich19919 & Hellebust19909Hellerharrison1992Hellinga1987 'Hellinga19927Hellinga1993 Helliwell1991( Hellman1987 Hellman1993 ( Helm1992 Helm19931 Helmersson1991 ) Helms1992! Helms1993 Hemker19933& Hemler1991 Hemminga19911Hemminga19911 NHemminga1991# Hemminga19919 *Hemminga1992Hemminga1992Hemminga19922Hemminga1992 +Hemmings1992 , Hemmingsen1988 n Hemmingsen1992 m Hemmingsen1992 - Hemmingsen1992  Hemmingsen1993  Hemmingsen1993 %^ Hemmingsen1993 .Hemphill1992]Hemphill19931 / Hemsley1989  Hendershot1993 * Hendershot1998 0 Henderson1992 1 Henderson1993 Henderson1994*T Henderson1998Hendrick1990 Hendrick1990Hendrick1991 2Hendrick1991 6Hendrick1993 7Hendrick1993 8Hendrick1995*Hendrick1997&} Hendrickson1996* Hendrickson1998 Hendrix1973 9 Hendrix1979@,HSp70,t,t,t,t,t,t-|t-t-t/"t/#t/%t/Jt/Kt/.t.t/t0jt13t14t15t1Ct1Nt1Pt1Rt1Tt1Ut1Wt1Xt1[t1ct1et1kt1ot1{t1t2vt2xt2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t3t3 t3t3t2t3t3t4Ct4ot4t4t4)t5ht5t5t5t5t5t5t5t5t5t6t6_t6t7t7t8t8t8 t6t8ct8tt8|t8t8t8tt9ttt2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2t2tt9ttN"c1273389085+,6W4818428555556L30976L5)5-4/4V4/45'48P'4 45o56365o9 967X7864015=7837 5=76 95556 7*78848Y85T08935T65U65U853536586U6216U894785129595I932887I85I87I88 9Z11942 Q557674575:75:9 "9E8316!1[1 Q15-4/4V4/45'4 4o55636o59 967X7=57837=57 69555 67*78848Y8T50893T56U56U585353658U6621U688512959I593288I588 9Z11Q 55767457:57:59" 9E831!61[1Q 14IM4L4M4Q4W4]4Y4X4f4e4d4b4^4n4l4j4i4o4p4q44z4{4|444444444444124)4s444444"44)441))44(#))))<Sciences1t)Qt1&t1!t/t0t0t1%t1t,t.t"t.Kt.Jt0~tt/ tett/t3t4}t4t4t4t4tt#t4tt4t4:t50t4t5t6t8t8t8t8t9 t9tj t0R t,t-t,t-t-t-t),t))t+Xt+_t'Ot+st)/t13't1D't1I't1N't1O't1Y't1Z't1e't1g't1m't1q't1|'t1|'t Fj^"Kim, D. 1991f`Modulation of Acetylcholine-Activated K+ Channel Function in Rat Atrial Cells by Phosphorylation$Journal of Physiology, LondonP 437133-155  Jund 3899ADRENERGIC-RECEPTOR KINASE ALPHA-SUBUNIT CHICK HEART FREE MEMBRANE GTP-BINDING PROTEINS MUSCARINIC RECEPTOR MUSCLE-CELLS OKADAIC ACID PIG CARDIAC MYOCYTES POTASSIUM CONDUCTANCE 3921"Kim, P.S. Bole, D. Arvan, P. 1992ASSOCIATION CELLS CHAIN BINDING-PROTEIN GLYCOPROTEINS IMMUNOGLOBULIN HEAVY-CHAIN INTRACELLULAR-TRANSPORT PRE-GOLGI SECRETORY PROTEINS TEMPERATURE VESICULAR STOMATITIS-VIRUSzTransient Aggregation of Nascent Thyroglobulin in the Endoplasmic Reticulum - Relationship to the Molecular Chaperone, BiPJournal of Cell BiologyB 118 3541-549 Augi 3909$Kim, J.K. Hollingsworth, M.J.m 1992ngINITIATION MESSENGER-RNA POLYSOMES PROTEINS RIBULOSE 1,5-BISPHOSPHATE CARBOXYLASE SEEDLINGS TRANSLATION2+Localization of Invivo Ribosome Pause SitesIAnalytical Biochemistryo 2061r183-188` Oct 3908.(Kim, J.H. Lee, Y.H. Kim, C.H. Park, C.Y. 1992yESCHERICHIA-COLI GROEL HYBRID PROTEINS LEADER PEPTIDE MEMBRANE MUTATIONS PREPROTEIN RECOGNITION SELECTION SIGNAL-SEQUENCEPIInvolvement of SecB, a Chaperone, in the Export of Ribose-Binding ProteinNJournal of Bacteriologyi 17416 5219-52276 Aug 3906"Kim, J. Adhya, S. Garges, S. 1992ADENOSINE-MONOPHOSPHATE RECEPTOR COMPLEX CONFORMATIONAL TRANSITIONS CONSTRUCTION CYCLIC-AMP DNA-BINDING DNA-PROTEIN INTERACTION GENE ACTIVATOR PROTEIN GENE REGULATION MUTATIONS PROTEIN CONFORMATION RESOLUTION TRYPTOPHAN SYNTHASE`YAllosteric Changes in the cAMP Receptor Protein of Escherichia-Coli - Hinge ReorientationE8920 9700-97040 15 OctVOProceedings of the National Academy of Sciences of the United States of AmericaO 3902<6Kim, E.E. Varadarajan, R. Wyckoff, H.W. Richards, F.M. 1992CRYSTALLOGRAPHIC REFINEMENT LEAST-SQUARES REFINEMENT MOLECULAR-DYNAMICS NEUTRON OCCUPANCY PROTEIN STRUCTURES RESOLUTION SOLVENT MOLECULES X-RAY REFINEMENTyRefinement of the Crystal Structure of Ribonuclease-S - Comparison with and Between the Various Ribonuclease-A Structureso Biochemistry3149 12304-12314 15 Dec 3901&Kim, D.H. Lee, Y.J. Corry, P.M.l 1992CELLS CLATHRIN COATED VESICLES COGNATE PROTEIN DNAK GENE HEAT-SHOCK PROTEINS SODIUM ARSENITE STRESS PROTEINS THERMOTOLERANCE UNCOATING ATPASEOLFConstitutive HSP70 - Oligomerization and Its Dependence on ATP Binding$Journal of Cellular Physiology 153a2353-361r Nov 39272,Kim, S. Landro, J.A. Gale, A.J. Schimmel, P. 1993~xBINDING ESCHERICHIA-COLI GLUTAMINYL-TRANSFER RNA IDENTIFICATION MOTIFS RECOGNITION RESOLUTION SEQUENCE SIMILARITIES SITEC-Terminal Peptide Appendix in a Class-I Transfer RNA Synthetase Needed for Acceptor-Helix Contacts and Microhelix Aminoacylatione Biochemistry3248 13026-13031o 7 Dec3 3925$Kim, P.S. Kim, K.R. Arvan, P.r 1993CELLS CONGENITAL GOITER ENDOPLASMIC-RETICULUM GLYCOSYLATION GOLGI INVITRO NEWLY SYNTHESIZED SECRETORY PROTEIN PULSE CHASE SECRETION TUNICAMYCINmb\Disulfide-Linked Aggregation of Thyroglobulin Normally Occurs During Nascent Protein Folding$American Journal of Physiology 265r3 C704-C711 Sep 3913Kim, K.S. Woodward, C. 1993LEAMIDE PROTON-EXCHANGE ISOTOPE EXCHANGE KINETICS LYSOZYME SPECTROSCOPYeProtein Internal Flexibility and Global Stability -Effect of Urea on Hydrogen Exchange Rates of Bovine Pancreatic Trypsin InhibitorO Biochemistry3237 9609-9613 21 Sep +`- 4)J('%&$ 517<5Benedetti, H. Lloubes, R. Lazdunski, C. Letellier, L. 1992COLICIN-A CROSS-RESISTANCE DNA DOMAINS K-12 LOCALIZATION MEMBRANES MITOCHONDRIA NUCLEOTIDE-SEQUENCE OUTER PORE CLOSING PROTEIN TRANSLOCATION TRYPSIN UNFOLDINGColicin-A Unfolds During Its Translocation in Escherichia-Coli Cells and Spans the Whole Cell Envelope When Its Pore Has Formed EMBO Journal112441-447 Feb1 519JCBenedict, R.C. Richey, B. Fall, L. Gill, S.J. Nagel, R.L. Wyman, J. 1981#ANTISICKLING AGENTS/PD [PHARMACOLOGY]. BINDING SITES. GELS #HEMOGLOBIN, SICKLE. HUMAN. OXYGEN/BL [BLOOD]. SOLUBILITY. SUPPORT U.S. GOV'T, NON-P.H.S. SUPPORT, U.S. GOV'T, P.H.S. THERMODYNAMICS #UREA/AA [ANALOGS AND DERIVATIVES]. UREA/PD [PHARMACOLOGY]>8Thermodynamics of anti-sickling agents with hemoglobin S 150o3423-434 15 Aug"Journal of Molecular Biology 5184.Benedict, R.C. Fall, L. Gill, S.J. Hedlund, B. 1981#GELS. HEMOGLOBIN, SICKLE/ME [METABOLISM]. HUMAN. KINETICS #MATHEMATICS. OXYHEMOGLOBINS/ME [METABOLISM]. PROTEIN CONFORMATION SERUM ALBUMIN, BOVINE. SOLUBILITY. SUPPORT, U.S. GOV'T, P.H.S@:The effect of non-binding molecules on the gelation of HbSBiophysical Chemistryl133P245-252 Jun 520&Benefraim, I. Bach, D. Shai, Y.a 1993ANALOGS CIRCULAR-DICHROISM FLUORESCENCE ENERGY-TRANSFER FORMING PEPTIDE ALAMETHICIN IONIC CHANNELS LIPID BILAYERS MEMBRANE-PROTEIN PHOSPHOLIPID-BILAYERS RAT UTERUS SENSITIVE SODIUM-CHANNELxqSpectroscopic and Functional Characterization of the Putative Transmembrane Segment of the minK Potassium Channel> Biochemistry329 2371-2377 9 Mar 521PIBenfenati, F. Valtorta, F. Rossi, M.C. Onofri, F. Sihra, T. Greengard, P. 1993ACYL CHAIN ORDER BIOLOGICAL-MEMBRANES F-ACTIN INDUCED MEMBRANE-FUSION MODEL MEMBRANES NEUROTRANSMITTER RELEASE PROTEIN-KINASE SELF-ASSOCIATION SQUID GIANT SYNAPSE TERMINAL-SPECIFIC PHOSPHOPROTEINlInteractions of Synapsin-I with Phospholipids -Possible Role in Synaptic Vesicle Clustering and in the Maintenance of Bilayer StructuresJournal of Cell BiologyP 1236 1845-1855 Dec 522Benham, C.J. Jafri, M.S. 1993COVALENT BOND TOPOLOGY CROSSLINKED LOOPS ENTANGLEMENTS GLOBULAR-PROTEINS KNOTS PANCREATIC TRYPSIN-INHIBITOR PROTEIN-STRUCTURE SPATIAL GEOMETRIC ARRANGEMENTS81Disulfide Bonding Patterns and Protein TopologiesUProtein ScienceI21 41-54o Jan<5Benie, A. J. Moser, R. Buml, E. Blaas, D. Peters, T.B 2003jdVirus-ligand interactions: identification and characterization of ligand binding by NMR spectroscopy.(Journal of the American Chemical Society 1251B 14-5.B Jan 812515488eng Journal ArticleB'Institute for Chemistry, University of Luebeck, Ratzeburger Allee 160, 23568 Luebeck, Germany, and Institute for Medical Biochemistry, Vienna Biocenter (VBC), University of Vienna, Vienna, Austria.BLEBenjamin, D.R. Robinson, C.V. Hendrick, J.P. Hartl, F.U. Dobson, C.M.# 1999<6Mass spectrometry of ribosomes and ribosomal subunits.VOProceedings of the National Academy of Sciences of the United States of America95 7391-7395  SJE 524 Benner, S.A. Gerloff, D.L. 1993DIVERGENCE EVOLUTION HOMOLOGOUS PROTEINS INDICATORS PATTERNS PROTEIN RECEPTOR SECONDARY STRUCTURE SEQUENCE STRUCTURE PREDICTION SUBUNIT TERTIARY TRYPTOPHAN SYNTHASEB s  iZ$REVIEWe)&e6e6e7e7e7e7e7e7e8)e88e8Ge8e8e8e8eee "e e5e,e-e)e++e01e4e4e4e4e4e4e4e5e5e5e5e5e5e5e5e6e6e6e6/e62e65e66e6?e6Le6me6oe6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e6e2qHTtp02ru2su2tu2uu2vu2wu2xu2yu2zu2{u2|u2}u2~u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u2u1ju1Vu2u2u2u2u2u2u2u000000 0000000000000000000000000000000000000000000000000000000000000000 0000000000000000000000000000000000000000000000000000000000000000 0000000000000000000000000000000000000000000000000000000000000000 0000000000000000000000000000000000000000000000000000000000000000 cleartomark [/N225/AdvP7C2E -1 TZ %!FontType1-1.0: AdvP7C34 1 13 dict begin /FontName /AdvP7C34 def /FontType 1 def /FontBBox {-169 -275 1010 734} readonly def /FontMatrix [0.001 0 0 0.001 0 0] readonly def /PaintType 0 def /FontInfo 12 dict du1PD1T21]21_21a21i21o21s21~212121212121212121212121212121222121212121212121212121212121212202?2222222222 222 2.222222222.2U2222222222222EopinionHssAs&sssYs(shss"sVsssQs*&s.s(s*s*sscss'ssss*s!s"s"ss#s$os*s&s)6s)5s Ks*os*ns(s(s*es* sUss*ps(s)s* s* s,ss,s,ms- s-6s-6s-6s-6s-6s-6sOOOOOO.M2)E-/2/+C///232426272;2=2?2B2@2C2D2E2I2G2N2M2ON2R/2Z2[2]2_2^2`2b2i2h0~2n2q2r2s2t2u2v2w2x222222222222221999 AHashemzadehbonehi1993 Hashim19922 Hashimoto1991 Hashimoto1991y Hashimoto1992 Hashimoto1992 - Hashimoto1993" Hashimoto1993" Hashimoto1994 Hashimoto1995  Hashimoto1996" Hashimoto1996  Hashizume1993 Haskell19910 Hasselbacher19929%U Hastie19911 Hasumi1988  Hata1991 Hata1992  Hata1993v  Hata1993v~ Hatakeyama1991 Hatanaka19922#rg, O. Reddy, P. Sutrina, S. Saier, M.H. Reizer, J. Kapadia, G. 1992ESCHERICHIA-COLI GRAM-POSITIVE BACTERIA MACROMOLECULAR CRYSTALLOGRAPHY PHOSPHOENOLPYRUVATE PHOSPHORYLATION REFINEMENT RESONANCE SECONDARY SUGAR PHOSPHOTRANSFERASE SYSTEM TERTIARY STRUCTURErkStructure of the Histidine-Containing Phosphocarrier Protein HPr from Bacillus-Subtilis at 2.0-A Resolution 896o 2499-2503o 15 MarVOProceedings of the National Academy of Sciences of the United States of America&2P&42&72&C2&B2&?2&H2*2&T2&V2&_2&`2&e2&r2&v2&s2&{2&~2&2&2&2&2&2&2&2&2'2+L2+S2+T2+V2+J2'L2+c2+d222)E2I2H2&22+p2+w2#2+}2+~2+2+2 2 2 2 2 2 2 2 2 2 2 2 2*u2*u2+2b+PRotein++++++++++++++++++*+!O  E+, K+')) J&-&+&++.} SElectIve lX l l' l  l  l l l lr l l( l l l l lB l lZ l[ l l l l l  l  l" l# l* l% l% l+ l, l-M l- l- l. l/  l0 l0 l2 l3 l4 l5 l6B l6 l7) l8K l8_ l8n l8 l9\ l9^ l ll l  lx l l l lX lZ l % l% l% l# l  l& lp l l l l l l!n l0 l5 l6+ l6B l6 l6 l7 l7) l77 l7I l7 l8z l8 l8 l  lyi iz i$ i$ i, i8z i ir i i167U0u0t000$0$0*0,0.0?0=0-01:02030506060 <000!0#0+0+00"0+5455W5(1 22d2#3334^446740]10]84X919 5 6 66(4 4)11H14X324H6/z660"00022/z56!7 7 8d8*888#81!1 Fersht19979& Fersht1997 & Fersht19979& Fersht19977& Fersht1997& Fersht19971& Fersht19977+ Fersht19979+ Fersht1997* Fersht1998 * Fersht19989) Fersht19988) Fersht19989) Fersht19989* Fersht1998 + Fersht19988 L Fertala1993 M Fesik1988 Fesik1988&  zPP> 6137 Phoenix, D.A. Pratt, J.M.0 1993TMAMPHIPHILIC HELIX ANCHOR MECHANISM MEMBRANE ANCHOR PENICILLIN BINDING PROTEINuvoMembrane Interaction of Escherichia-Coli Penicillin Binding Protein-5 Is Modulated by the Ectomembranous Domaine FEBS Letters 32203215-218 17 May 6135F@Phoenix, D.A. Kusters, R. Hikita, C. Mizushima, S. Dekruijff, B. 1993ACIDIC PHOSPHOLIPIDS AMINO-TERMINAL REGION CYTOPLASMIC MEMBRANE ENDOPLASMIC-RETICULUM LIPID INTERACTIONS MODEL MEMBRANES PLASMA-MEMBRANE POSITIVE CHARGE PRECURSOR PROTEINS SECA PROTEINOmpF-Lpp Signal Sequence Mutants with Varying Charge Hydrophobicity Ratios Provide Evidence for a Phosphatidylglycerol-Signal Sequence Interaction During Protein Translocation Across the Escherichia-Coli Inner Membrane&Journal of Biological Chemistryr 268S23 17069-17073 15 Aug 6134\VPhoenix, D.A. Dewolf, F.A. Staffhorst, R.W.H.M. Hikita, C. Mizushima, S. Dekruijff, B. 1993ACIDIC PHOSPHOLIPIDS ADRIAMYCIN COMPLEX MITOCHONDRIA NEGATIVELY CHARGED PHOSPHOLIPIDS PHOSPHATIDYLGLYCEROL PRECURSOR PROTEINS PROTEIN TRANSLOCATION SIGNAL-SEQUENCEPhosphatidylglycerol Dependent Protein Translocation Across the Escherichia-Coli Inner Membrane Is Inhibited by the Anti-Cancer Drug Doxorubicin -Evidence for an Electrostatic Interaction Between the Signal Sequence and Phosphatidylglycerol FEBS Letters 324S1113-116. 7 Jun- 6138ZSPicard, D. Khursheed, B. Garabedian, M.J. Fortin, M.G. Lindquist, S. Yamamoto, K.R. 1990BINDING DOMAIN CELLS DIVERGENT GAL1-GAL10 PROMOTER DNA HEAT-SHOCK PROTEIN HORMONE LIVER GLUCOCORTICOID RECEPTOR SACCHAROMYCES-CEREVISIAE TRANSCRIPTION YEASTHAReduced Levels of hsp90 Compromise Steroid Receptor Action Invivo7 Nature 348 6297166-168u 8 Nov- 6139JCPiccardo, P. Dagenais, A. Cuello, A.C. Stpierre, S. Nalbantoglu, J. 1993ngBETA BRAIN CELLS CORE PROTEIN DOMAIN LOCALIZATION MESSENGER-RNA NERVE GROWTH-FACTOR NEXIN SECRETED FORMIxqAn Antibody Against the Alzheimer's Disease Amyloid Precursor Protein Recognizes Distinct Conformational IsoformsoHistochemistry995a347-3530 May 6140ngPiccione, E. Case, R.D. Domchek, S.M. Hu, P. Chaudhuri, M. Backer, J.M. Schlessinger, J. Shoelson, S.E. 1993EGF-RECEPTOR GAP GROWTH-FACTOR RECEPTORS KINASE-ACTIVITY PDGF RECEPTOR PHOSPHOLIPASE-C PHOSPHOTYROSINE PROTEIN SIGNAL TRANSDUCTION TYROSINE PHOSPHORYLATIONtrlPhosphatidylinositol 3-Kinase p85 SH2 Domain Specificity Defined by Direct Phosphopeptide/SH2 Domain Binding Biochemistry3213 3197-3202 6 Apr 6141B;Picken, R.N. Mazaitis, A.J. Maas, W.K. Rey, M. Heyneker, H.t 1983$ENTERO-TOXIN GENE SEQUENCE STBXRNucleotide sequence of the gene for heat-stable enteortoxin II of Escherichia coliInfection and Immunity42269-275SvoPickersgill, R. Varvill, K. Jones, S. Perry, B. Fischer, B. Henderson, I. Garrard, S. Sumner, I. Goodenough, P. 1994\UMaking a small enzyme smaller; removing the conserved loop structure of hen lysozyme. 347199-202 FEBS Letters 6142&Pickett, S.D. Sternberg, M.J.E.e 1993CHI-ANGLES CONFIGURATIONAL ENTROPY ENERGY FREE-ENERGY GLOBULAR-PROTEINS HYDROPHOBICITY LYSOZYME MOLECULAR-DYNAMICS MUTAGENESIS PREDICTION PROTEIN MOBILITY RECOGNITION SECONDARY STRUCTURE STABILITY SURFACENGEmpirical Scale of Side-Chain Conformational Entropy in Protein Folding6 2313N825-839 5 Jun-"Journal of Molecular Biology 6144D>Picking, W.D. Odom, O.W. Tsalkova, T. Serdyuk, I. Hardesty, B. 1991tmBACILLUS-SUBTILIS BINDING-SITE ERYTHROMYCIN ESCHERICHIA-COLI RIBOSOMES RIBONUCLEIC-ACIDS SUBUNIT TRANSFER-RNAXRThe Conformation of Nascent Polylysine and Polyphenylalanine Peptides on Ribosomes&Journal of Biological Chemistry 2663 1534-1542 25 Jan HIJdKZLMpNOPQ`thods, those requiring the coat protein for the cell-to-cell spread (comoviruses) and those not having this requirement (tobamoviruses). The previously unsuspected relationship between the movement proteins of RNA and DNA viruses havi 447760Li, Z.M. Glibowicka, M. Joensson, C. Deber, C.M. 1993`ZBACTERIOPHAGE DNA DYNAMICS ESCHERICHIA-COLI FD M13 MEMBRANE MUTAGENESIS MUTATIONS SEQUENCE`YConformational States of Mutant-M13 Coat Proteins Are Regulated by Transmembrane Residues&Journal of Biological Chemistry 2687 4584-4587 5 Mar 4476 Li, Z.H. Srivastava, P.K. 1993 BINDING-PROTEINS CANCER IMMUNITY CHAPERONE CLASS-I MOLECULES ENDOPLASMIC-RETICULUM ESCHERICHIA-COLI GLUCOSE-REGULATED PROTEINS HEAT-SHOCK HISTOCOMPATIBILITY COMPLEX ANTIGENS HSP90 MHC CLASS-I PEPTIDE PEPTIDE BINDING SHOCK COGNATE PROTEIN STRESS-INDUCED PROTEINSNpjTumor Rejection Antigen gp96/grp94 Is an ATPase -Implications for Protein Folding and Antigen Presentation EMBO Journal128n 3143-3151n Aug 4475Li, Z. Hermans, J. 1993@9Calculation of the Pitch of the alpha-Helical Coiled CoilS172S217-218I Oct0*Proteins: Structure, Function and Genetics 4474Li, Z. Hermans, J. 1993ALPHA-HELIX AMINO-ACIDS BINDING CHEMICAL-SHIFTS COILED-COIL CONFORMATION CONFORMATIONAL STABILITY FREE-ENERGY SIMULATIONS GCN4 HELIX PROPENSITY LEUCINE-ZIPPER MOLECULAR-DYNAMICS PEPTIDES PROTEINPJMolecular Dynamics Study of Structure and Stability of a Model Coiled Coil164384-392 Augr0*Proteins: Structure, Function and Genetics 4472NHLi, Y.T. Hsieh, Y.L. Henion, J.D. Senko, M.W. McLafferty, F.W. Ganem, B. 1993^XCOILED-COIL COMPLEXES DNA-BINDING ELECTROSPRAY-IONIZATION FOS GCN4 JUN PROTEIN SUBSTRATERKMass Spectrometric Studies on Noncovalent Dimers of Leucine Zipper Peptidesy.(Journal of the American Chemical Society 11518 8409-8413P 8 Sep 4471,&Li, Y. Luo, L.Z. Rasool, N. Kang, C.Y. 1993ANTIGEN CD4 ENVELOPE GLYCOPROTEIN ESCHERICHIA-COLI EXPRESSION HTLV-III/LAV INSECT CELLS N-LINKED GLYCANS SYNCYTIUM FORMATION T4 MOLECULE VIRUS TYPE-1 GP120yngGlycosylation Is Necessary for the Correct Folding of Human Immunodeficiency Virus-gp120 in CD4 Binding Journal of Virology5671584-588 Jan8 4470 Li, X.H. Carrington, J.C. 1993rlBINDING IDENTIFICATION IMPORT INCLUSION PROTEIN LOCATION PRODUCTS REGION TRANSLATION TRANSLOCATION VIRUS-RNAztNuclear Transport of Tobacco Etch Potyviral RNA-Dependent RNA Polymerase Is Highly Sensitive to Sequence AlterationsVirology 1932951-958 Apr 4466Li, S.C. Deber, C.M. 1993RKCHAINS GLYCINE PROTEIN RESIDUES SECONDARY STRUCTURE SIGNAL TRIFLUOROETHANOLoPeptide Environment Specifies Conformation - Helicity of Hydrophobic Segments Compared in Aqueous, Organic, and Membrane EnvironmentsO&Journal of Biological Chemistry  268 31 22975-22978 5 Nov 4462,%Li, M.H. Fan, P. Brodsky, B. Baum, J. 1993AMINO-ACID SEQUENCE CIRCULAR-DICHROISM MOLECULAR-DYNAMICS MULTIPLE-QUANTUM COHERENCE NUCLEAR MAGNETIC-RESONANCE PROLINE PROTEINS PROTON PULMONARY SURFACTANT APOPROTEIN SPECTROSCOPYxr2-Dimensional NMR Assignments and Conformation of (Pro-Hyp-Gly)(10) and a Designed Collagen Triple-Helical Peptide Biochemistry3229 7377-7387 27 Jul 4448@9Li, H.M. Hanson, C. Fuchs, J.A. Woodward, C. Thomas, G.J. 1993BIOMOLECULES CONFORMATION LASER RAMAN MODEL COMPOUNDS PROTEINS REDUCED FORM SECONDARY STRUCTURE SPECTRA TRYPTOPHAN VIRUS STRUCTUREDetermination of the pKa Values of Active-Center Cysteines, Cysteines-32 and Cysteines-35, in Escherichia-Coli Thioredoxin by Raman Spectroscopy Biochemistry3222 5800-5808 8 June^660v00 00_0 00"00 -0)0"E0"0#B0&%0+f0+0^0.i0/01f0102'0304060607!0709D0`00.0 0 0 L0 m0b00e00*g00)0+_0%00101f070_000068080B0 010C00W00002'04'00112$v33/443/43/43/42sAnd2te2ze2|e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e2e1>e2e2e2e2e2e2e te2e2eee2e2e2e2e2e2e2e2e2e2e2e2e3e3e3e3e3e320023333333'33(33)33*33+33,33-33.33/33033133233333433533:33933833733@33;33<33=33>33?33A33B33C33D33E33F33G33H33I33J3333P33O33N33K33M33R33Q3233323233d33c33b33a33`33_33^33]33\33[33Z33Y3,1997,8-8*8)S8)R8(8*08-$8*8-(8)8&8(8*C8-A8-[8-a8-c8-e8-g8-j8-k8-8-8-8-8.8. 8. 8.8.8.8.8. 8.'8-Q8+D8.t8.s8.{8.8.8.8+8-8+G8(8/8/#8&8-8'S8*8-p8).8)"8(8/=8+z8-8.8.8H`Kuntzoooooosu4}ugi*opp*pp"p#Dp#Fp$bp4p persztoch r r  r r r  f ferschmid%sier%kes f ryszewski.ramitsu *ototnda0eepaianh,h-h8hUharammmHm motot/ttan7y*yanoo#o#o+To6o,o8$o ochkina* a6 a aDdatkk/i ~}d|$6F2VD.,/{zJ,wZxNy 3404*#Hwang, Y.W. Carter, M. Miller, D.L. 1992ALPHA-SUBUNIT AMINO-ACIDS EF-TU FUNCTIONAL SITES GTP-BINDING DOMAIN GUANINE NUCLEOTIDES H-RAS P21 ONCOGENE PROTEIN SACCHAROMYCES-CEREVISIAE TRIPHOSPHATE CONFORMATIONevpThe Identification of a Domain in Escherichia-Coli Elongation Factor-Tu That Interacts with Elongation Factor-Ts&Journal of Biological Chemistry 26731 22198-22205a 5 Nov 3403Hwang, T.L. Shaka, A.J. 1992^XC-13 NMR CONFORMATION H-1-NMR SPECTRA NOE SPECTROSCOPY OFFSET ROESY SELECTIVE EXCITATION`YCross Relaxation Without TOCSY - Transverse Rotating-Frame Overhauser Effect SpectroscopyE.(Journal of the American Chemical Society 114e8 3157-3159 8 Apr 3400*$Hwang, C. Sinskey, A.J. Lodish, H.F. 1992BOND FORMATION CATALYZED FORMATION MICROSOMAL-MEMBRANES PROTEIN DISULFIDE ISOMERASE RAT-LIVER RIBONUCLEASE SYSTEM THIOL TRANSLOCATION TRANSPORTF@Oxidized Redox State of Glutathione in the Endoplasmic ReticulumScience 257t 5076 1496-1502` 11 SepHwang, T.-L. Shaka, A.J. 1998Multiple-pulse mixing sequences that selectively enhance chemical exchange of cross-relaxation peaks in high-resolution NMR spectrap$Journal of Magnetic Resonance 135|280-287 SJE 3405:3Hyberts, S.G. Goldberg, M.S. Havel, T.F. Wagner, G. 19922,3-DIMENSIONAL STRUCTURE BIOLOGICAL MACROMOLECULES COMPARISON X-RAY CORRELATION SPECTROSCOPY CRYSTAL-STRUCTURE DISTANCE GEOMETRY EGLIN-C ELASTASE INHIBITOR LEECH HIRUDO-MEDICINALIS MOLECULAR-STRUCTURE NMR NUCLEAR MAGNETIC-RESONANCE SERINE PROTEINASE INHIBITOR-2 SOLUTION STRUCTURE SUBTILISIN CARLSBERGThe Solution Structure of Eglin-c Based on Measurements of Many NOEs and Coupling Constants and Its Comparison with X-Ray StructuresProtein ScienceC16.736-751 Jun 3406F?Hyman, A.A. Salser, S. Drechsel, D.N. Unwin, N. Mitchison, T.J.  1992ASSEMBLY INVITRO BINDING CELLS ELONGATION GUANOSINE 5'-TRIPHOSPHATE HYDROLYSIS INSTABILITY MECHANISM MICROSCOPY POLYMERIZATION TUBULIN-NUCLEOTIDE INTERACTIONSngRole of GTP Hydrolysis in Microtubule Dynamics -Information from a Slowly Hydrolyzable Analogue, GMPCPPL$Molecular Biology of the CellG3e10 1155-1167 Octd*$Ibarra-Molero, B. Sanchez-Ruiz, J.M. 1996A model-independent, nonlinear extrapolation procedure for the characterization of protein folding energetics from solvent-denaturation data. Biochemistry35 14689-14702 JAH*$Ibarra-Molero, B. Sanchez-Ruiz, J.M. 1997hbAre there equilibrium intermediate states in the urea-induced unfolding of hen egg-white lysozyme? Biochemistry36 9619-9624 JAH :3Ibarra-Molero, B. Makhatadze, G. I. Matthews, C. R.r 2001\VMapping the energy surface for the folding reaction of the coiled-coil peptide GCN4-p1 Biochemistry403i719-31.f11170389 JAHeZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=11170389rIbba, M. 2002$DEAD-end job for RNA chaperoneTrends Biochem Sci279. 446  Sept'ibba.1@osu.edu 3407 Ichihara, S. Mizushima, S. 19870*CLONING GENE PROTEIN REVIEW SECA SECRETIONA review with 22 refs. 0372-1566ENHFunctional analysis of cloned genes: genes involved in protein secretion Taisha2412 1141-1149Nagoya 464, Japan  3408 Ichihara, S. Mizushima, S. 1988>7PEPTIDASE PROTEASE PROTEIN REVIEW SECA SECRETION SIGNALdrkA review with 30 refs. on the role of signal peptidases and signal peptide peptidases in protein secretion.n 0370-8241$Protein secretion and protease Saishin Igaku434i736-741Nagoya 464, Japan 3409F?Ichimura, T. Shindo, Y. Uda, Y. Ohsumi, T. Omata, S. Sugano, H.  1993COMPONENTS ENDOPLASMIC-RETICULUM IDENTIFICATION LIVER PROTEIN TRANSLOCATION RAT RAT-LIVER RECEPTOR RIBOSOME RIBOSOME-BINDING PROTEIN ROUGH MICROSOME~xAnti-(p34 Protein) Antibodies Inhibit Ribosome Binding to and Protein Translocation Across the Rough Microsomal Membrane FEBS Letters 326 1-3241-245 12 Jul \2 [X Z Y,%Stader, J. Benson, S.A. Silhavy, T.J. 1986jdKinetic analysis of lamB mutants suggests the signal sequence plays multiple roles in protein export&Journal of Biological Chemistry2 26132 15075-150809 7465A quant. assay was developed to measure the rate of processing of precursor LamB into mature protein and used to characterize 10 previously isolated and 3 new lamB signal sequence mutants. The LamB signal sequence serves a complex function. Five types of signal sequence defects were obsd.: (1) a strong kinetic defect resulting from alteration of the secondary structure in the putative .alpha.-helical region in the hydrophobic core, (2) a strong, or (3) a weak kinetic defect due to placement of a charged residue in the hydrophobic core, (4) decreased synthesis of LamB, and (5) both a decrease in synthesis and a strong kinetic defect. The effect of an extragenic suppressor, prlA4, on the rate of processing pLamB contg. signal sequence mutations was also examd. and compared to the rates in wild-type strains. The prlA4 increases the rate of processing in some, but not all, mutants having a kinetic defect while having no effect on the decreased synthesis seen in mutants of types 4 and 5. 0021-92582 7467Stader, J. Silhavy, T.J. 1988ZTDuring its localization to the outer membrane, Escherichia coli LamB possesses distinctive biochem. properties as it passes through the cytoplasmic membrane. Because LamB entered this dynamic state with an attached signal sequence and leaves after cleavage, this export-related form of LamB is called the early-translocation form (et-LamB). 0021-9193  1704o 1973-1974r4.A progenitor of the outer membrane LamB trimerJournal of Bacteriology 74660)Stader, J. Gansheroff, L.J. Silhavy, T.J. 1989TNAnal. of >100 extragenic suppressors of the lamB14D signal-sequence mutation (changes Val in the hydrophobic core region at position 14 to Asp) has revealed alterations that appear to lie at prlA (secY) and secA (prlD), 2 loci known to be mutable to suppressor alleles, and a new suppressor termed prlG. One allele of the new suppressor class, prlG1, was characterized in some detail. This suppressor counteracts, to some degree, the export defect conferred by a variety of signal-sequence mutations in 2 different genes, lamB and malE. Genetic anal. shows that the dominant suppressor mutations are linked tightly to, and probably allelic with, the gene secE. This result, coupled with data obtained with conditional-lethal alleles of secE, argues strongly that SecE is an important component of the cellular protein export machinery in E. coli. 0890-936937| 1045-1052srlNew suppressors of signal -sequence mutations, prlG, are linked tightly to the secE gene of Escherichia coliGenes and Development 7468 Stader, J.A. Silhavy, T.J. 1990PIA review with 108 refs. on problems encountered in secreting heterologous proteins from Escherichia coli and some of the successes which have been achieved to date. Topics discussed include the rational for secreting proteins in E. coli and problems involved in their secretion, protein targeting pathways in E. coli, the secretion of hemolysin, enterotoxins, and colicin, the definition of secretion in E. coli, prokaryotic exoprotein secretion and export and/or secretion of eukaryotic proteins from E. coli including .beta.-endorphin, human growth hormone, human epidermal growth factor and superoxide dismutase, and mouse-human Fab proteins, and novel approaches for secretion of foreign proteins. The effects of host strain, growth temp., length of induction, and cotranscription on secretion of heterologous proteins is also discussed. 0076-6879HBEngineering Escherichia coli to secrete heterologous gene products 185 (Gene Expression Technol.)166-187Methods in Enzymology516 Nov  5415nhMutter, M. Tuchscherer, G.G. Miller, C. Altmann, K.H. Carey, R.I. Wyss, D.F. Labhardt, A.M. Rivier, J.E. 1992BUNDLE PROTEIN CONSTRUCTION DENOVO DESIGN FOLDING UNITS HELICAL PROTEIN HELICHROME PHASE PEPTIDE-SYNTHESIS POLYPEPTIDE SECONDARY STABILIZATION~xTemplate-Assembled Synthetic Proteins with 4-Helix-Bundle Topology - Total Chemical Synthesis and Conformational Studies.(Journal of the American Chemical Society 1144S 1463-1470S 12 Feb5' Engineering5' l5' l5' l5' l6 ' l6' l6)' l6K' l6j' l6n' l6' l6' l6' l7' l7"' l7;' l7<' l7>' l7' l7' l7' s7' s7' s8' s8=' s8F' s8X' s8]' s8f' s8i' s8' s8' s8' s8' s8' s8' s8' s7s4^landhh~h) h) h) H) e) e) e) e) e)G e)$ e) e) e& e)6 e)5 e), e)- e)* e+X e+^ e+c e+e e+f e& e)D e+p e'M e+w e+ e+ e+ e-| e+ e+t e+Y e+s e)/ e)e)e-ze1'e1'e1'e1'e3&'e7C'e8'e8'e8'eIerHH H& H< Hg e ef+ e& eD) ep+ eM' ew+ e+ e+ e+ e|- e+ et+ eY+ es+ e/) e)e)ez-e1'e1'e1'e1'e&3'eIerHH H& H< Hg eZSEattt t tt7tt6tTtttl $g ggg>bbSbb3b b"b#b$b6_bbrayy6o!fookychristgarl$Ri8e+iedi*ing8SSRy man rrrchE oE EEEeEEEEeE1E E"E+E0.E3E4E4E5KE5E E EiZabaaaaaa a ca a a a a a a <a a a a a aa:a*aWa**aiaaaAa@anaaaaaaaaEaQaPaOaNaLaRaWaa^abapaa^a_a5aTaaaaaaaa* @8 xAmiNo P P P P P P P P6folding6o6(o6)o62o64o67o68o6<o6?o6@o6Co6Go6Io6Jo6Ro6So6To6Wo6ho6no6to6wo6|o6}o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o6o7o7o7o7o7o7o7o7o7o7o7o7o111111)1O1111 1&11111/11*1o11111111 1 1 1 1 1 1 1 1 1!/1!C1!Y1!1!1)H1"1#1#E1#f1$)1$b1$1%X1%1%1%1&1&L1&K1&O1&{1+k1+l1I1 1,11Robinson;ssssssssssssss&sssss!fs" s#2s${s+s\s s,s-=s-s-s-s-s-s.1sss-s.s/ s*o/]o)o/o.Ho.=o/o0oo3"o3,o3o+o6o6o7 o7!o9Do7o/ onuclease vson c#ckwith, J. Taura, T. Ueguchi, C. Akiyama, Y. Ito, K. 1990DNA EXPORT GENE MEMBRANE-VESICLES MUTATION RIBOSOMAL-PROTEIN OPERON SECRETION SIGNAL-SEQUENCE SUPPRESSION TEMPERATURE TRANSLOCATIONJCCharacterization of Cold-Sensitive secY Mutants of Escherichia-ColiiJournal of Bacteriologyu 17212 7005-7010t Deco 276@9Baba, S. Takahashi, T. Kasama, T. Fujie, M. Shirasawa, H.  1993ALZHEIMERS-DISEASE AMINO-ACID SEQUENCE BETA-FIBRILLOSES CO6Havem6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k6k7k7k7k7k7k7k7 k7!k7%k7+k7,k74k7:k7;k7<k7@k7Ak7Lk7Pk7ak7bk7dk7ek7fk7hk7jk7kk7ok7pk7qk7rk7tk7uk7xk7yk7{k7k7k7k7k7klainedo2ored6 y"y5f5023ka "AVORABLEa u& e'Q e7 e8A eaeduurabledolda/o34A bledoldao/3A % @ #use#d#d$d$+d$ud%d)d,3d,Rdbd,ddOd-dd$d$d,Td.d.dd/Sd/d/d0(d0d1&d1%d1ddIHSp70*s s%s4)s6s6?s6_s6|s6s6s6s6s6s6s6s6s6s6s6s6s7s7.s76s7=s7s7s6s8cs8ts8|s8s18s222222 -2*28S%SA1%C1 2 83~3*8 829z34n590Q QQQjQiQSQQ}Q{Q(QQQQ|Q|Q|QN ٰ ٰ p  ٰ p p ٰ%d[@ ٰp 0 H ' ٰ W ݀0 0 D N ٰ ٰ p  ٰ p p ٰ%d[@zarus, R.A.   1997hbEngineering Hyperactive Variants of Human Deoxyribonuclease I by Altering Its Functional Mechanism( Biochemistry  36& 6624-6632  HBDNase I, DNA scission, double scission, hyperactive enzyme variant"Pan, T. Fang, X. Sosnick, T. 1999\UPathway modulation, circular permutation and rapid RNA folding under kinetic control.q"Journal of Molecular Biology 286721-731d SJEF9 :|<6=>`?^@ABCDE3F45 4449*$Li, H.M. Sullivan, T.D. Keegstra, K. 1992IMPORT RECEPTOR INVITRO OUTER-MEMBRANE PEA-CHLOROPLASTS PHOSPHATE TRANSLOCATOR SEQUENCE SPINACH-CHLOROPLASTS THYLAKOID LUMEN TRANSIT PEPTIDE TRANSPORTInformation for Targeting to the Chloroplastic Inner Envelope Membrane Is Contained in the Mature Region of the Maize Bt1-Encoded Protein&Journal of Biological Chemistry 26726 18999-19004 15 Sep 444682Li, G.C. Li, L.G. Liu, R.Y. Rehman, M. Lee, W.M.F. 1992ATP-BINDING CHINESE-HAMSTER FIBROBLASTS CONSTRUCTION EXPRESSION GENE INDUCTION LOCALIZATION RECOVERY RESISTANT VARIANTS RETROVIRUS STABLE EXPRESSION THERMAL-RESISTANCE THERMOTOLERANCEpiHeat Shock Protein hsp70 Protects Cells from Thermal Stress Even After Deletion of Its ATP-Binding Domain&896 2036-2040 15 MarVOProceedings of the National Academy of Sciences of the United States of America 4438Li, C. Clarke, S.8 1992AGING ASPARAGINYL RESIDUES CARBOXYL METHYLTRANSFERASE DEAMIDATION DEGRADATION GENERAL RESISTANCE INDUCED CROSS PROTECTION KATF L-ISOASPARTYL RESIDUES NUCLEOTIDE-SEQUENCE PROTEIN L-ISOASPARTYL METHYLATION REPAIR SPONTANEOUS PROTEIN DEGRADATIONA Protein Methyltransferase Specific for Altered Aspartyl Residues Is Important in Escherichia-Coli Stationary-Phase Survival and Heat-Shock Resistance8920 9885-98890 15 OctVOProceedings of the National Academy of Sciences of the United States of Americac 4473Li, Z. Castellino, F.J. 1992{ACTIVATION ANTICOAGULANT BLOOD CLOT LYSIS CA-2+ BINDING COFACTOR FACTOR PLASMA PROTHROMBIN STRUCTURAL REQUIREMENTS THROMBINInfluence of Specific gamma-Carboxyglutamic Acid Residues on the Integrity of the Calcium-Dependent Conformation of Human Protein-Ca&Journal of Biological ChemistryS 267436 26078-26084V 25 Dec 446982Li, X. Sutcliffe, M.J. Schwartz, T.W. Dobson, C.M. 1992AMPHIPHILIC SECONDARY STRUCTURES DISTANCE GEOMETRY NEUROPEPTIDE-Y NUCLEAR MAGNETIC-RESONANCE PROTEINS PROTON CHEMICAL-SHIFTS RECEPTOR-BINDING SPECTROSCOPY TRYPSIN-INHIBITOR X RAY ANALYSIS[d]Sequence-Specific H-1 NMR Assignments and Solution Structure of Bovine Pancreatic Polypeptidei Biochemistry314 1245-1253 4 Feby 4468(!Li, X. Smith, R.A.G. Dobson, C.M.M 1992ACTIVATOR AROMATIC H-1-NMR SPECTRUM HUMAN-PLASMINOGEN KRINGLE-4 LYSINE-BINDING NUCLEAR MAGNETIC-RESONANCE PROTEINS RESOLUTION SINGLE-CHAIN UROKINASE SPECTROSCOPY TWO-DIMENSIONAL NMRb[Sequential H-1 NMR Assignments and Secondary Structure of the Kringle Domain from Urokinasen Biochemistry3140 9562-9571c 13 Oct 446760Li, S.L. Yan, P.F. Paz, I.B. Fujitayamaguchi, Y. 199295,000-DALTON SUBUNIT AUTOPHOSPHORYLATION BASIC POLYCATIONS BINDING GROWTH FACTOR-I HUMAN PLACENTAL MEMBRANES MONOCLONAL-ANTIBODIES OWN RECEPTOR PHORBOL ESTERS PHOSPHORYLATIONcHuman Insulin Receptor beta-Subunit Transmembrane/Cytoplasmic Domain Expressed in a Baculovirus Expression System - Purification, Characterization, and Polylysine Effects on the Protein Tyrosine Kinase Activity Biochemistry3149 12455-12462n 15 Dec 4465Li, S.C. Deber, C.M. 1992ALANINE ALPHA-HELIX AMINO-ACID SEQUENCE BACTERIOPHAGE BACTERIORHODOPSIN CIRCULAR-DICHROISM CONFORMATION GLYCINE HELIX-FORMING TENDENCIES HYDROPHOBIC RESIDUES HYDROPHOBIC SEGMENTS LIPID VESICLES M13 COAT PROTEIN MEMBRANES MICELLES PEPTIDE STABILIZATIONeTNInfluence of Glycine Residues on Peptide Conformation in Membrane Environments<5International Journal of Peptide and Protein Research640 3-4243-248-Sep-Oct 4464Li, S.C. Deber, C.M. 1992ALPHA-HELIX AMINO-ACIDS BACTERIORHODOPSIN CIRCULAR-DICHROISM CONFORMATION HELIX-FORMING TENDENCIES HYDROPHOBIC SEGMENT LIPID BILAYERS MEMBRANE PEPTIDE PROTEIN RESOLUTION SEQUENCE SPECTROSCOPY STABILITY haGlycine and beta-Branched Residues Support and Modulate Peptide Helicity in Membrane Environments  FEBS Letters 311e3217-220 26 Oct 4463&Li, R.H. Shi, Y.G. Thomas, J.O.e 1992ASP GLU ASP IDENTIFICATION IMPORT INVITRO LOCATION SIGNAL MAMMALIAN-CELLS PORE COMPLEX T-ANTIGEN TRANSLOCATION TRANSPORT SIGNALSRKIntracellular Distribution of a Nuclear Localization Signal Binding Protein- Experimental Cell Research 202e2355-365e OctP 4461Li, M. Wong, S.L.1 1992ANTIGEN DNAK GENE ESCHERICHIA-COLI EXPRESSION HEAT-SHOCK PROTEINS LAMBDA MYCOBACTERIUM-TUBERCULOSIS NUCLEOTIDE-SEQUENCE RNA-POLYMERASE SIGMA-FACTORNHCloning and Characterization of the groESL Operon from Bacillus-SubtilisJournal of Bacteriology  17412 3981-3992  Junt 4460 Li, M. Jan, Y.N. Jan, L.Y. 1992DELAYED RECTIFIER PROPERTIES EPSILON-SUBUNIT EXCITABLE CELLS FUNCTIONAL EXPRESSION HETEROMULTIMERIC CHANNELS K+ CHANNEL MAMMALIAN BRAIN MUSCLE ACETYLCHOLINE-RECEPTOR RAT-BRAIN XENOPUS OOCYTESppjSpecification of Subunit Assembly by the Hydrophilic Amino-Terminal Domain of the Shaker Potassium ChannelScience 257 5074 1225-1230 28 Aug 4459Li, M. Ishibashi, T. 1992"ASSAY ESCHERICHIA-COLI HEARTReversible Conformational Changes of Rat Liver Fatty Acid Binding Protein Following Lipid Binding -Circular Dichroic and Nuclear Magnetic Resonance AnalysisBiomedical Research135335-341 Oct 445782Li, L.Y. Falzone, C.J. Wright, P.E. Benkovic, S.J. 1992|vBINDING CATALYSIS CONFORMATIONAL-CHANGES CRYSTAL-STRUCTURES FOLATE METHOTREXATE MUTAGENESIS NADPH SITE TERNARY COMPLEXtnFunctional Role of a Mobile Loop of Escherichia-Coli Dihydrofolate Reductase in Transition-State Stabilization Biochemistry3134 7826-7833 1 Sep0 4454B;Li, L. James, G. Hellerharrison, R. Czech, M.P. Olson, E.N.P 1992FGF Inactivates Myogenic Helix-Loop-Helix Proteins Through Phosphorylation of a Conserved Protein Kinase-C Site in Their DNA-Binding Domains Cell717R 1181-1194T 24 Dec 4439*$Li, C.W. Moore, D.S. Rosenberg, R.C. 1993BINDING CHEMICAL MODIFICATION DIETHYLPYROCARBONATE ENZYME ETHOXYFORMIC ANHYDRIDE INACTIVATION PROTEINS RESIDUES SITE SODIUM DODECYL-SULFATERf`Circular Dichroism Studies of Diethyl Pyrocarbonate-Modified Histidine in Hen Egg White Lysozyme&Journal of Biological Chemistryf 26815 11090-11096i 25 May 8 6 7 5 4 3/X 2 103-,0 03"Gupta, R. S. Golding, G. B. 1993~wEvolution of HSP70 gene and its implications regarding relationships between archaebacteria, eubacteria, and eukaryotes J Mol Evol376 573-5828114110XRhttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=8114110'HBDepartment of Biochemistry, McMaster University, Hamilton, Canada. Gupta, R.S.p 1994`YIdentification of a GroES (cpn10)-Related Sequence Motif in the GroEL (cpn60) Chaperonins33591-595  288560Biochemistry and Molecular Biology International$Gupta, R. Yadav, S. Ahmad, F.d 1996ZSProtein stability: urea-induced versus guanidine-induced unfolding in metmyoglobin  Biochemistry35 11925-11930 JAHGupta, R. Ahmad, F.  1999d]Protein stability: Functional dependence of denaturational Gibbs energy on urea concentration Biochemistry38 2471-2479 JAHRD=Gurevich, V.V. Pokrovskaya, I.D. Obukhova, T.A. Zozulya, S.A. 1991DPreparative in vitro mRNA synthesis using SP6 and T7 RNA polymerases    Analytical Biochemistryd 195207-213q JAH 2887@:Gurrath, M. Muller, G. Kessler, H. Aumailley, M. Timpl, R. 1992ARG GLY ASP CELL-ADHESION COHERENCE-TRANSFER CYCLOSPORINE-A FIBRONECTIN INTEGRINS MOLECULAR-DYNAMICS NMR-SPECTROSCOPY RECOGNITION ROTATING-FRAME\VConformation/Activity Studies of Rationally Designed Potent Anti-Adhesive RGD Peptides& European Journal of Biochemistry 210t3911-921e 15 Dec 28884-Gursky, O. Badger, J. Li, Y.L. Caspar, D.L.D.b 1992D>1.5-A RESOLUTION DETECTOR MODEL PEPTIDE PIG INSULIN REFINEMENTLEConformational Changes in Cubic Insulin Crystals in the pH Range 7-11TBiophysical JournalI635e 1210-1220  NovGursky, O. Aleshkov, S.  2000<Temperature-dependent b-sheet formation in b-amyloid Ab(1-40) peptide in water: uncoupling b-structure folding from aggregation    + , 6 7 [ \ Biochim Biophys Acta 14761! 93-102Amyloid beta-Protein/*chemistry Buffers Circular Dichroism Electrophoresis Peptide Fragments/*chemistry Protein Folding *Protein Structure, Secondary Solubility Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. Temperature Waterhttp://www.ncbi.nlm.nih.gov/cgi-bin/Entrez/referer?http://www.elsevier.com:80/cgi-bin/cas/tree/store/bbapro/cas_sub/browse/browse.cgi%3fyear=2000&volume=1476&issue=1&aid=3603320074565 SJE 2889 Gussakovsky, E.E. Haas, E. 1992BOVINE PANCREATIC TRYPSIN INHIBITOR CIRCULAR-DICHROISM SPECTROSCOPY CONFORMATIONAL STATES FLUORESCENCE INTERMEDIATE MOLTEN-GLOBULE STATE OPTICAL ROTATORY DISPERSION PROTEIN FOLDING REFOLDING PATHWAY SIDE-CHAINShbThe Compact State of Reduced Bovine Pancreatic Trypsin Inhibitor Is Not the Compact Molten Globule FEBS Letters 308i2146-148 17 Aug 2890,&Gustchina, A. Weber, I.T. Wlodawer, A. 1991.(Molecular modeling of the HIV-2 protease 306R549-5534-Advances in Experimental Medicine and BiologyA 2891^XGustke, N. Steiner, B. Mandelkow, E.M. Biernat, J. Meyer, H.E. Goedert, M. Mandelkow, E. 1992ALZHEIMERS-DISEASE DEPENDENT KINASE DISEASE DOMAINS IDENTIFICATION ISOFORMS LOCALIZATION LOCATION MICROTUBULE NEUROFIBRILLARY TANGLES PAIRED HELICAL FILAMENTS PHOSPHORYLATION PROLINE-DIRECTED KINASE TAU-PROTEIN TUBULIN|uThe Alzheimer-Like Phosphorylation of tau-Protein Reduces Microtubule Binding and Involves Ser-Pro and Thr-Pro MotifsB FEBS Letters 3072N199-205 28 Jul 2893"Gutheil, W.G. McKenna, C.E.h 1992tnUnique and Independent Parameters (UIP) Formulation for Thermodynamic Models of Complex Protein Ligand SystemsBiophysical Chemistry452 171-179 DecB 2892 Gutheil, W.G. 1992piThermodynamic Model of Cooperativity in a Dimeric Protein - Unique and Independent Parameters FormulationBiophysical Chemistry 452181-191 DecT 2894Guthrie, B. Wickner, W. 1990Trigger factor is an abundant cytosolic protein of Escherichia coli which can stabilize proOmpA for in vitro translocation across inner membrane vesicles. The gene encoding E. coli trigger factor was isolated and sequenced, allowing construction of strains in which the expression of trigger factor is readily regulated. No defect in the in vivo rate of synthesis or secretion of proOmpA was found in trigger factor-depleted cells. The primary physiol. defect in trigger factor-depleted or -overproducing cells is an enrichment of filamented cells. Filamentation of the trigger factor-overproducing strain is suppressed by a multicopy plasmid expressing the essential division gene ftsZ, suggesting that trigger factor has an important role in cell division. 0021-9193. 17210 5555-55620rkTrigger factor depletion or overproduction causes defective cell division but does not block protein export5Journal of Bacteriology5Sci5e5e5e5e5e5e5e5e5e5e5e6e6e6e6'e6*e6:e6?e6@e6Fe6Ue6be6ge6je6se6te6ze6e6e6e6e6e6e6e6e6e6e6e6e7e7e7e7 e71e73e74e7;e7Ce7Le7e7e7e7e7e7e7e7e7e7e8 e8e8e8e Klimov, D.K.d 1998@9Fishing for folding nuclei in lattice models and proteinsLFolding and Design3L R112-R1187 December 15@ SJE(Pi) a P 0Thirumalai, Pnd D. K. Klimov (1998). "Fishing for folding nuclei in lattice models and proteins." Folding and Design 3: R112-R118. @ H  0%'( Pbd  0      0 0   7Inm777777777777777777777777777777777777777777777777777777777777777ween  Kuhlman, B., L. Luisi, et al. (1998). "Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9." Journal of Molecular Biology 284: 1661-1670. tric   ain, wheeas    Vertebrate U y y y y( y y k y# y y` yz yJ yN I7c I7 s7 x7 x7x'x8ICALyy%y!sss s'ss&s-s+s-s2&s4s4s6s8=sss*ssRs s_sss`sIs-ssMsssssss$s!Ds#qs)(s)-s'Os   @ p@k @ K EndNo P pk k0 \ ߰ Q l@ ,|H`|H~_HJ`J p l \ K m hh &f`&~   m    q m0 l*A CORRELATED\ s V sD s& s] s s# s) s%' s+o s)/ s0 s5 s64 s6 s6 s6 s73 s7C s7z s7 s7 s8? s8F s8R s8S s8q s8 s8 s  s i  i$n i$ i3 i i i"u i#  i)) i i'P i0 i6 i6 i7 i8j i'[ing o o  o  oT oW o&) o5 o  ons: s s s s s s@ s s s seatmentndsZi ibUTYRINfY fluoRoethanolgger&mer% NUCLEOTIDESl phosphateleT TNAo+'obepomyosina sha$p ueyL ypanosomes=sint At tic;ophan%; s s0 s#sai ong+urupa uberculosisulinM(s 77-84 13 Jul 4912,&Matsuyama, S. Fujita, Y. Mizushima, S. 1992NGCDNA 383960Kennedy, D.F. Crisma, M. Toniolo, C. Chapman, D. 1991AMINOISOBUTYRIC-ACID ATOMIC RESOLUTION CHAIN-LENGTH CONFORMATIONAL-ANALYSIS LINEAR OLIGOPEPTIDES SECONDARY STRUCTURES SIGNAL PEPTIDES SOLID-STATE VIBRATIONAL ANALYSIS X RAY DIFFRACTIONStudies of Peptides Forming 3(10)-Helices and alpha-Helices and beta-Bend Ribbon Structures in Organic Solution and in Model Biomembranes by Fourier Transform Infrared Spectroscopy Biochemistry3026 6541-6548 2 July10_00040\000 30 0 0 H0 Y0 0 0 0 n0l00[000200&0000!00000000000d000)000$0H00040`00T0000]00 0H00 0 0 Sequenceh/h~hh'th4hh]r r Vs sasscdddldd<dddFdBd&Ad(d*ddd&td*ddKs t tb t, t "tialr$b r5rdiesnen+pinsum-Yy ylt'tsrvveral'H H2a*abanwlloway*pedredweet(Os_s's s$rmanEQibIRE'ftssoSnPock[rSrQr )r r Qr1}Uid1~P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P1P5 6 46 p6 r6 v6 6 6 6 6 6 6 6 6 6 6 6!6!6!B6![6!b6!6!6!6!6!6!6!6!6!6!6!6!6"6"&6"66"86"B6"D6"V6"\6"o6"y6"6"6"6# 6#6#h6#6#6#6#6#6#6#6#6#6#6$6$"6$66$@65819$Ottaway, C.A. Wetlaufer, D.B.B 1970.'Library currently receives this journalaVOLight-scattering contributions to the circular dichroism of particulate systemsA.'Archives of Biochemistry and BiophysicsE 139r2 257-264 AugeOtting, G. Wthrich, K. 1989~wStudies of protein hydration in aqueous solution by direct NMR observation of individual protein-bound water molecules. 111 1871-1875.(Journal of the American Chemical Society+domainI+S+S+S+S+S+S*S,S+FS)S+S+S,*S,2S,7S(S+AS,GS,HS,IS,MS,OS,QS,cS,dS,lS,vS,S,S,S,S,S,S*S+S#vS*yS]S+;SSqS SS*S,S-uS-S-S-OS-S-S.S.!S.?SS-S.bS.S.S.S.S.S8946456467)8888# 0{0.000)206'87q'87'88'68 688'/86134692922288e3- 2.09E00%02271623'/39%4_9,T5.009000900 01 13z27393z3T357x2707x5 58T9 566 6!60\666W666 46 .6)B666#66q666F6 6!6!6dremains <r_r#r^r)$rMrlr+Xr+_r+prr+sr6r6*r63r6r7.r7Fr7r7r7r81r84r8lr8r*rkableo o"C y)' y)5 y)- y+Y y0 y6 y6 y6> y6b y7 y7 y82 y8? y8 y8 y- y6 e_ ee e el e+g e+o eN u0 u0 u0 u6I u6 u7- u7: u7 u7 u7 u7 u7 u84 u8m u8 u+uteediosrowski# i0igyngton! m$5 m  m+oiscent0 m63 m7 m)mersNN'NANTS*bodeledTEd :v 9v8v3vablele eiee]eeeeSe)e)e)e)e Translocase t t t)V t)U t)C t t tv t)L t t t)N t$ t$ t* t/6 t t0b t0 t0 t0 t0 t0 t0 t0 t0 t0 t0 t); t6 t7h t7l t7 t7 t8m t t t t t t t t t  t t+\ t0 t0 t0 t0 t0 '0 '+  '0 '6 '6 '6 '7h '7j '7k '7w '7 '7 '7 '7 '7 '7 '7 '89 '8` '8m '0 'st te* d  dN d d d0 d0 d6 d7s d7w d7 d d1`' university1c' k1e' k1f' k1g' k1m' k1q' k1s' k1y' k1z' k1{' k1|' k1}' k1~' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k1' k2s' k2t' k2u' k2v' k2x' k2z' k2z' k2z' kConnecting to host... Connecting to host... Searching for: [chen*[AUTH]+AND+samuelson*[AUTH]]. Sending message to server... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving references 1 - 3... Sending message to server... Connecting to host... Client message sent The Host closed the connection. Retrieving reference number 4... Sending message to server... &8/22*2 \2 2 2 2 G2 2 22f22(2 2 2d2s222(222y2"2T22Q2*22@22*2 2"2#2)2$/2*2'%2* 2)2,z2,{2,2,2-*2- 2-B2-R2-^2-u2-2-2-2-2.,2.B2.u2.2-2-2-2000J Sasaki19899 Sasaki1990 ? Sasaki1990 : Sasaki19911m Sasaki19919 Sasaki1992< Sasaki1992  Sasaki19922 Sasaki19939 Sasaki1993  Sasaki1994 / Sasaki19999 Sasaoka1992 Sasaoka1993 Sasisekharan19633 Sasisekharan19681 Sass2000 Sassedwight19902 Sassi2002' Sather1994 bSathyanarayana1992"G Sato19900 Sato1990v# Sato19929 SajBiology u Suu=u u$u u6u7{u_u u u u guuuuu u u!u uu)5u4u6u7Ku7u7u7u7u8u8`u8ou%@u)u)u)u)u)u)u)u)u)u)u)u)u)u)5u)+u)*u+fu+hu+ju+pu+wu+xu+u11'u15'u1?'u1@'u1A'u1F'u1J'u1M'u1O'u1U'u1W'u1Z'u1_'u1e'u1t'u1v'u1w'u1w'u1w'u1w'uAntonino1991Antonino1993 Antonny1993 Antuch1993 ! 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Hardy, D. Kaback, H.R. 1992COOH TERMINUS CYTOPLASMIC SIDE ESCHERICHIA-COLI EXPRESSION LAC CARRIER PROTEIN MEMBRANE-VESICLES MONOCLONAL-ANTIBODIES PROTEOLIPOSOMES STABILITY TRANSPORTrlEvidence That the Final Turn of the Last Transmembrane Helix in the Lactose Permease Is Required for Folding&Journal of Biological Chemistryf 267r10 6471-6474` 5 Apr&McKenzie, H.A. White, F.H., Jr. 1991HLysozyme and a-lactalbumin: structure,FEBS Letters 325m3167-172 5 Juln 3454Byamaeeda}4'gasaki1i'kimUmotoiP) u$ u3 uM" u" u0 u0 u0 u ura n2 n6 n5 n4 n3 n8 n: n9 n n n n^ n  n# n. nnagam( m"miov o;o"kN+k/kkas<ssshimau u  eO  e e e e eC2 e eroa utaa'ura=yyy>yamaa$completeiddd d#d%d)'d+gd+d+d&d4d5d6Pd6d6d6d6d7d7Xd7d8pd8d1d lE l$ l l7 llyx  x8 x* xq x s& s) s O s x s  s s s s# s" s#z s), s s+r s+{ s+~ s0 s s6@ s6t s6 s6 n7{ n7} n7 n7 n7 n7 n8 n8 n8? n8} n8 n6 n8 n6nessss i6 iTionE x x6A x6P x6 x7r x7 x8 x8 xx/UGe)eweyeeeeeeees,) s sr+ s{+ s~+ s0 s s6 s@6 ss iTionE x xx/UGe)eweyeeeeeeeeNegaja a6ate~siveaBaa6a 2a aa aaeaa*a aa=alaaa5aDa"ga,>a,aa)"a2a2a4:aaKav o y glCleeeeg)km,fi$%6+e#aaaaja a6ate~siveaBaa6a2 aa a aaeaa*a aa=alaaa5aDag"a>,a,aa")a2a2a:4aaKav o yg lCleeeeg)km,fi$%+6e#lvOmpfORRR#RR4RR$&R%R#Ruu%uuu#uu&VT Vura nnnnnnnanbnn!n%nn2nCCCC CC(CCC%C*C1C7C8C;CHCxCCCCCCCCCCC*C#C3C<C(C(C(C(CR4RR#Ruuuu#uu Vura nnnnnnnnanbnnnCCC CC(CCC%C*C1C7C8C;CHCRCxCCCCCCCCCCCC*C*C#C3C<CEC(C&. Hurley1996.t Hurley19976 Hurley2003 Hurme1992] Hurst1992_ Hurst1993O Hurt19900E Hurwitz1993) Hurwitz19959 Huryeva2004NHusgafvelpursiainen1993 Huskisson1992 Husmeier19922 Hussey1992# Hussey19922d Hustedt19938 Hut19863R Hutagalung2002eHutchins1991 Hutchinson1989f Hutchinson1989  Hutchinson1992  Hutchinson1992 g Hutchinson1993 %E Hutchinson1993 h Hutchinson1994 & Hutchinson1997 -j Hutchinson1997$+ Hutchinson1998- Hutchinson1999/, Hutchinson19991 Hutchinson2001;46 Hutchinson20026 Hutchinson2002 Hutchison1992j Hutchison1992i Hutchison1992 Hutchison1992k Hutchison1993l Huth1991vv Huth19919m Huth1992vn Huth1993v*; Huth1997v Huttinger1993"A Huttner1990o Huttner1991) Huttner1992 Hutton1990 qHuyghues-Despointes1992sHuyghues-Despointes1993pHuyghues-Despointes1993.Huyghues-Despointes1999/qHuyghues-Despointes19996:Huyghues-Despointes19992=Huyghues-Despointes2001 Huynh-Dinh1996i{ Huynhdinh1992z Huynhdinh1992| Huynhdinh1993t Hvidt1966Hvizdala1989 Hwang1990u Hwang1990v Hwang1991 Hwang1992 Hwang1992y Hwang1992x Hwang1992w Hwang1992 Hwang1992 Hwang1992% Hwang1993 Hwang1993, Hwang19988 Hwang19988 Hwang20018= Hwang2003j Hyams1990& Hyams1991  Hyberts1992# Hyberts1992z Hyberts1992"f Hyde19929 Hyde19929 Hyde1993! Hyman1991 Hyman1992 Hyman1992{ Hyman19924# Hyndman20016f Hyndman20017a Hyndman20014 Hyndman2002' Hynes1992s Hyvonen1996s Iacopetta1993 v Iacopetti1992' Ianson19919,/ Ibarra-Molero1996. Ibarra-Molero19973 Ibarra-Molero20007 Ibarra-Molero20002V Ibarra-Molero20016F Ibba2002U Ibea199291,Ibrahimi1981>Ibrahimschneck1991|Ichihara1987}Ichihara1988!Ichihara19888Ichikawa19922!Ichikawa1992Ichikawa1993 Ichikawa1993!Ichimura19911~Ichimura1993%Ichinose1993 Ichiyanagi1992 6 Ichtchenko2002!b Ida1990'Igarashi1991vIgarashi1993, Igloi19928Ignatova2003g Igo1989 Igo1990-$ Igumenova1997!b Ihara1990C Ihara1992 Ihara1992$( Ihara1992 Ihara1992 Ihara1993 Ihara1993% Ihara1993 Ihler1991 Ihler1991' Iihara19919 - Iijima19939 Iio1992* Iiri1998v Iitaka19911 Iizuka199390 Ikai1971w- Ikai1973- Ikai1973- Ikai19739 Ikawa1992 Ikeda1990 * Ikeda1991 Ikeda1991 , Ikeda1992 Ikeda19924} Ikeda2002f Ikedasaito19933C Ikegawa1992Ikeguchi1985Ikeguchi1986Ikeguchi1986Ikeguchi1990Ikeguchi1992!Ikeguchi19930Ikeguchi1997*Ikeguchi1998,sIkeguchi1998-Ikeguchi19992BIkeguchi19990 Ikeguchi200004FIkeguchi20022!z Ikehara1990 Ikehara1991 Ikehara1992{ Ikehara1993 Ikehara1994! Ikehura19881( Ikemoto2002 " Ikenaka1991"7 Ikenaka1991* Ikura1989 Ikura1989 Ikura1990 Ikura1990 Ikura1990 Ikura1990 Ikura1990S Ikura1990 Ikura1990'[ Ikura1991 Ikura1991 Ikura1991 Ikura1991 Ikura1991T Ikura1991 ? Ikura1991 Ikura1992 Ikura1992 Ikura1992  Ikura1992) Ikura1992 Ikura1993 Ikura1993 Ikura1994+ Ikura1995- Ikura1997) Ikura1998+t Ikura1998,E Ikura19986 Ikura1998- Ikura19992D Ikura20006G Ikura20002 Ikura20026k Ikura2002 Ikuta1993 Ikuta1993 Ikuta19932eHutchins1991 Hutchinson1989f Hutchinson1989  Hutchinson1992  Hutchinson1992 g Hutchinson1993 E% Hutchinson1993 h Hutchinson1994 & Hutchinson1997 j- Hutchinson1997$+ Hutchinson1998- Hutchinson1999,/ Hutchinson19991 Hutchinson2001;64 Hutchinson20026 Hutchinson2002 Hutchison1992j Hutchison1992i Hutchison1992 Hutchison1992k Hutchison1993l Huth1991vv Huth19919m Huth1992vn Huth1993v;* Huth1997v Huttinger1993A" Huttner1990o Huttner1991) Huttner1992 Hutton1990 qHuyghues-Despointes1992sHuyghues-Despointes1993pHuyghues-Despointes1993.Huyghues-Despointes1999q/Huyghues-Despointes1999=2Huyghues-Despointes2001 Huynh-Dinh1996i{ Huynhdinh1992z Huynhdinh1992| Huynhdinh1993t Hvidt1966Hvizdala1989 Hwang1990u Hwang1990v Hwang1991 Hwang1992 Hwang1992y Hwang1992x Hwang1992w Hwang1992 Hwang1992  Hwang1992% Hwang1993 Hwang1993, Hwang1998j Hyams1990& Hyams1991 Hyberts1992# Hyberts1992z Hyberts1992f" Hyde19929  Hyde19929 Hyde1993! Hyman1991 Hyman1992 Hyman1992{ Hyman1992#4 Hyndman20014 Hyndman2002' Hynes1992s Hyvonen1996s Iacopetta1993v  Iacopetti1992' Ianson19919/, Ibarra-Molero1996. Ibarra-Molero19973 Ibarra-Molero2000V2 Ibarra-Molero2001U Ibea19929,1Ibrahimi1981>Ibrahimschneck1991|Ichihara1987}Ichihara1988!Ichihara19888Ichikawa19922!Ichikawa1992Ichikawa1993 Ichikawa1993!Ichimura19911~Ichimura1993%Ichinose1993 Ichiyanagi1992 b! Ida1990'Igarashi1991vIgarashi1993, Igloi1992 Igo1989 Igo1990$- Igumenova1997b! Ihara1990C Ihara1992 Ihara1992($ Ihara1992 Ihara1992 Ihara1993 Ihara1993% Ihara1993 Ihler1991 Ihler1991' Iihara19919- Iijima19939 Iio1992* Iiri1998v Iitaka19911 Iizuka199390 Ikai1971w- Ikai1973- Ikai1973- Ikai19739 Ikawa1992 Ikeda1990* Ikeda1991 Ikeda1991, Ikeda1992 Ikeda1992}4 Ikeda2002f Ikedasaito19933C Ikegawa1992Ikeguchi1985Ikeguchi1986Ikeguchi1986Ikeguchi1990Ikeguchi1992!Ikeguchi19930Ikeguchi1997*Ikeguchi1998s,Ikeguchi1998-Ikeguchi1999B2Ikeguchi1999 0Ikeguchi20000F4Ikeguchi20022z! Ikehara1990 Ikehara1991 Ikehara1992{ Ikehara1993 Ikehara1994! Ikehura1988(1 Ikemoto2002" Ikenaka19917" Ikenaka1991 * Ikura1989 Ikura1989 Ikura1990 Ikura1990 Ikura1990 Ikura1990 Ikura1990S Ikura1990 Ikura1990[' Ikura1991 Ikura1991 Ikura1991 Ikura1991 Ikura1991T Ikura1991? Ikura1991 Ikura1992 Ikura1992 Ikura1992 Ikura1992) Ikura1992 Ikura1993 Ikura1993 Ikura1994+ Ikura1995- Ikura1997) Ikura1998t+ Ikura1998E, Ikura1998- Ikura1999D2 Ikura20002 Ikura2002 Ikuta1993Ikuta199339-2$4b1j0/R-B,4X+J*)('9L,&Jansens, A. van Duijn, E. Braakman, I. 2002RKCoordinated nonvectorial folding in a newly synthesized multidomain protein9Science> 298 5602 2401-2403 Dec 20 KSR9 3537:4Jansson, M. Thurmond, R.L. Trouard, T.P. Brown, M.F. 1990nhCHOLESTEROL H-2 NMR LYSOLECITHIN MODEL MEMBRANE NMR P 31 NMR PHOSPHATIDYLCHOLINE RESONANCE SYSTEMS WATERMagnetic Alignment and Orientational Order of Dipalmitoylphosphatidylcholine Bilayers Containing Palmitoyllysophosphatidylcholine6&Chemistry and Physics of Lipids 54 3-4p157-170- Jun 353881Jarabak, R. Westley, J. Dungan, J.M. Horowitz, P.N 1993CHAPERONE EFFECT CYANIDE DETOXICATION DENATURED RHODANESE ERYTHROCYTES MOLTEN GLOBULE FORMS PROGRAM RHODANESE FOLDING SERUM-ALBUMIN SULFUR-CYANOLYSIS SULFURTRANSFERASE THIOSULFATE>8A Chaperone-Mimetic Effect of Serum Albumin on Rhodanese(!Journal of Biochemical Toxicology-8t1 41-48e MarP 3539f`Jarjour, W. Mizzen, L.A. Welch, W.J. Denning, S. Shaw, M. Mimura, T. Haynes, B.F. Winfield, J.B. 199065-KILODALTON MYCOBACTERIAL ANTIGEN ANTIBODIES AUTOANTIBODIES BACTERIAL HEAT-SHOCK PROTEIN IDENTIFICATION RECEPTOR SYSTEMIC LUPUS-ERYTHEMATOSUS T-CELLS TUBERCULOSISb\Constitutive Expression of a Groel-Related Protein on the Surface of Human Gamma/Delta-Cells& Journal of Experimental Medicine 172e6 1857-1860 1 Deci 3540TNJarjour, W.N. Jeffries, B.D. Davis, J.S. Welch, W.J. Mimura, T. Winfield, J.B. 1991ANTIBODY-LEVELS ARTHRITIS BORRELIA-BURGDORFERI CELLS GROEL PROTEIN HEAT-SHOCK PROTEIN LYMPHOCYTE-T CLONES MYCOBACTERIAL SYNOVIAL-FLUID SYSTEMIC LUPUS-ERYTHEMATOSUSoUnselected sera from patients with various rheumatic, inflammatory bowel, and autoimmune skin diseases (n = 268) were examined against human cell lysate by immunoblotting procedures, to determine the prevalence of autoantibodies to stress proteins (heat-shock proteins) hsp60 (homolog of Escherichia coli groEL and mycobacterial 65K antigens), hsp73, and hsp90. Using standard, sensitive and specific assay conditions, IgG and IgM autoantibodies to these stress proteins were not demonstrable, or were detected infrequently, in sera from control subjects (n = 36) and from patients with rheumatoid arthritis, Sjogren's syndrome, ankylosing spondylitis, Reiter's syndrome, systemic lupus erythematosus, and systemic sclerosis. Autoantibodies to hsp60 were relatively more common (greater-than-or-equal-to 20% of sera) in patients with mixed connective tissue disease, polymyositis/dermatomyositis, psoriatic arthritis, inflammatory bowel disease, epidermolysis bullosa acquisita, and bullous pemphigoid. Anti-hsp73 autoantibodies were detected in 20% or more of the sera from patients with Lyme disease and ulcerative colitis. Taken together, these data extend the spectrum of autoimmune and inflammatory diseases in which humoral anti-stress protein autoreactivity develops. However, the paucity of humoral autoreactivity to stress proteins in patients with systemic lupus erythematosus and rheumatoid arthritis argues against a direct role of anti-stress protein autoantibodies in the pathogenesis of these disorders.ngAutoantibodies to Human Stress Proteins - A Survey of Various Rheumatic and Other Inflammatory DiseasesCArthritis and Rheumatism349L 1133-1138% Sep0 3541Jarnik, M. Aebi, U. 1991COMPONENTS ENVELOPE GLYCOPROTEINS IDENTIFICATION INVITRO LAMINA OOCYTE GERMINAL VESICLES PROTEIN IMPORT TRANSLOCATION TRANSPORTF@Toward a More Complete 3-D Structure of the Nuclear Pore Complex$Journal of Structural BiologyO 107v3291-308l DecbPIJaroniec, C. P. MacPhee, C. E. Astrof, N. S. Dobson, C. M. Griffin, R. G.s 2002XRMolecular conformation of a peptide fragment of transthyretin in an amyloid fibrilProc Natl Acad Sci U S A9926 16748-16753w Dec 2412481032 JAH?lehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12481032S'jcDepartment of Chemistry and Center for Magnetic Resonance, Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139; Cavendish Laboratory, University of Cambridge, Madingley Road, Cambridge CB3 0HE, United Kingdom; and Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, United Kingdom. 3544 Jarosik, G.P. 199082INCOMPLETE ESCHERICHIA GENE MUTATION OPERON SECA X UnavailablefhbGeneration and characterization of dominant mutations in the geneX-secA operon of Escherichia coli 0*State Univ. New York; Stony Brook, NY, USA 179 3542 Jarosik, G.P. Oliver, D.B. 1991xrATP BINDING COMPONENT EXPORT GENE-PRODUCT MEMBRANE-VESICLES PROTEIN TRANSLOCATION SECRETION SECY24 DEFECT SEQUENCELEIsolation and Analysis of Dominant secA Mutations in Escherichia-ColiJournal of Bacteriology 1732860-868 Jan Jarpe, M.A. Johnson, H.M.  1993Stable Conformation of an Interferon-gamma Receptor Binding Peptide in Aqueous Solution Is Required for Interferon-gamma Antagonist Activity2+Journal of Interferon and Cytokine Research@132@ 99-103 Apr 35452,CIRCULAR-DICHROISM EPITOPE MOUSE SPECIFICITY 3547"Jarrett, J.T. Lansbury, P.T. 1992xrACID AGGREGATION ALANINE ALZHEIMERS-DISEASE CONFORMATION CONGO RED FRAGMENTS KINETICS PEPTIDES SECONDARY STRUCTUREAmyloid Fibril Formation Requires a Chemically Discriminating Nucleation Event - Studies of an Amyloidogenic Sequence from the Bacterial Protein OsmBt Biochemistry3149 12345-12352h 15 Dec 35460)Jarrett, J.T. Berger, E.P. Lansbury, P.T.P 1993D>CONFORMATION DEPOSITION FRAGMENTS PEPTIDES SECONDARY STRUCTUREThe Carboxy Terminus of the beta-Amyloid Protein Is Critical for the Seeding of Amyloid Formation -Implications for the Pathogenesis of Alzheimer's Diseaser Biochemistry3218 4693-4697 11 MayXQJarrett, N. M. Djavadi-Ohaniance, L. Willson, R. C. Tachibana, H. Goldberg, M. E.t 2002lfImmunochemical pulsed-labeling characterization of intermediates during hen lysozyme oxidative folding Protein Scii11112584-95  Nov712381842 JAHalehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12381842c'xrUnite de Repliement et Modelisation des Proteines (CNRS URA 2185), Institut Pasteur, 75254 Paris Cedex 15, France. 3548<5Jarvis, D.L. Summers, M.D. Garcia, A. Bohlmeyer, D.A. 1993AMINO-ACID SEQUENCE CHAIN BINDING-PROTEIN GLUCOSE-REGULATED PROTEIN HIGH-LEVEL EXPRESSION HONEYBEE PREPROMELITTIN HUMAN INSULIN-RECEPTOR INSECT CELLS NUCLEAR POLYHEDROSIS-VIRUS NUCLEOTIDE-SEQUENCE RECOMBINANT BACULOVIRUSInfluence of Different Signal Peptides and Prosequences on Expression and Secretion of Human Tissue Plasminogen Activator in the Baculovirus Systemc&Journal of Biological Chemistrys 268r22 16754-16762 5 AugJas, GS Kuczera, K 2004Equilibrium structure and folding of a helix-forming peptide: Circular dichroism measurements and replica-exchange molecular dynamics simulationsBiophysical Journal87 3786-3798 KSR 3550B Muller1992 1 Muller19922 Muller19921, Muller19921 Muller1992 !( Muller1992$ Muller19920 Muller1992 / Muller1992 . Muller1992 - Muller1992 | Muller19922E Muller19922  Muller19921Y Muller19931 Muller1993 0 Muller19939$ Muller199393 Muller1993 2 Muller1993  Muller19939' Muller1996 0\ Muller199716 Muller19979+\ Muller19987{ Muller199990 Muller200005 Muller200007 Muller200000 Muller20017 Muller20012 Muller200203 Muller2002<5_ Muller20027| Muller20025 Muller200327 Muller200334Muller-Fahrnow19915 Muller-Frohne1997C Mulleresterl1993T Mullerhill1993a"mMullertaubenberger1992 Mullins19905 Mullins1993 ~ Mullins1996( Mullins1997' Mullock1993 GMulthaup19899 KMulthaup199093Multhaup200208Multhoff20037 Multigner1992 5 Mulvey1975 + Mulvey199298 Mumby1990? Mumby19921S Mun20012 Mun20026vMunagala2001Munakata1985Munakata1986 Munch19939 Mundigl19935Mundorff20032! Mundy1992%Munekata1992/[Munekata200000!Munekata20000 Munholland1991  Munier19929 Munier1993 : Munier1993 + Munk19939 Munn19922 Munns1992 Munoz1992+ Munoz19987N Munoz19982a Munoz19993 Munoz20016( Munoz20014Z Munoz2002- Munro1986> Munro1991 Munske1995  Munson1992 , Munson1998? Muntz1992- Muoz19944 Muoz19944 Muoz19944 Muoz1994; Muoz1995= Muoz1996< Muoz1996) Muoz1997( Muoz19974 Muoz19970 Muoz2001  Murad1980 Murai1980@ Murai1993AMurakami1990BMurakami1991CMurakami1992DMurakami19937Murakami2002 Muraki1992E Muraki1992 Muraki199297 Muraki19949FMuramoto1990GMuramoto1992 Murant19919 Murant19929 Muraoka1993 Murase1993 % Murase1993 I Murase1993 H Murase1993  Murata19922!K Murata1992J Murata1992 "; Murata19939 Murata19933K Murata1993 6_Murawski19952Murawski1999DMurayama19933L Murby1991d Murchie1993*9 Murchie1997 Murcko199397x Murcko19988% Murdoch1993 Murgia19939 Murgue1993y"Murialdo1981&Murialdo19921% Muro19921 Murofushi1990 Murofushi1991" Murphy1982 Murphy19833M Murphy1983 N Murphy1986  Murphy1988eO Murphy1990 Murphy1991 Murphy19919[ Murphy19911Q Murphy1991 % Murphy19911 Murphy1992 "= Murphy1992 V Murphy1992 U Murphy1992 T Murphy1992 S Murphy1992  Murphy1993 Murphy1993 W Murphy1993X Murphy1993 # Murphy1993 ] Murphy1995 ) Murphy1995 Z Murphy1995 2 Murphy1995< Murphy1996r- Murphy1999 2 Murphy200002 Murphy200102 Murphy2001 1 Murphy200223 Murphy200225m Murphy2003+j Murphy EC1997 Murray1981 7 Murray1991 7 Murray1991 Mullins1996( Mullins1997' Mullock1993 GMulthaup19899 KMulthaup199097 Multigner1992 5 Mulvey1975 8 Mumby1990? Mumby1992Munakata1985 Munch19939 Mundigl1993! Mundy1992%Munekata1992 Munholland1991  Munier19929 Munier1993 : Munier1993  Munn19922 Munns1992 Munoz1992; Munoz1995= Munoz1996< Munoz1996> Munro1991 Munske1995  Munson1992 ? Muntz1992) Muoz1997( Muoz1997  Murad1980 Murai1980@ Murai1993AMurakami1990BMurakami1991CMurakami1992DMurakami1993 Muraki1992E Muraki1992 Muraki199297 Muraki19949 Murant19919 Murant19929 Muraoka1993 Murase1993 % Murase1993  Murata19922!K Murata1992"; Murata19939 Murata19933Murayama19933d Murchie1993*9 Murchie1997 Murcko19939% Murdoch1993 Murgia19939 Murgue1993y"Murialdo1981&Murialdo19921 Murofushi1990 Murofushi1991" Murphy1982 Murphy19833 Murphy1988e Murphy1991 Murphy19919[ Murphy19911 Murphy1992 "= Murphy1992  Murphy1993 Murphy1993 W Murphy1993] Murphy1995 ) Murphy1995 Z Murphy1995  Murphy1996r Murray1981 7 Murray1991 ) SpECIficity TQ T T T T T T T T TM T T  T $ T @ T B T  T& T  T  T  T  T T/ T T* T8 T` T T T T T T T T> Tg T T T T TM T TQ Tq T T T2 T T T T T T TX T TW Tj Tm T T $ T!d T6Isv6a6a6a6a6a6!a6"a6#a6%a6&a6'a6)a6+a6-a60a61a63a64a65a68a6:a6;a6<a6=a6>a6?a6@a6Aa6Ba6Ca6Da6Ga6Ia6Ka6La6Ma6Na6Oa6Pa6Qa6Ra6Sa6Ta6Ua6Wa6Xa6Ya6Za6[a6\a6]a6^a6_a6`a6aa6ba6ea6ga6ha6ha6ha6ha6ha/ METABOLISM2 t3& t4o t4u t4x t4 t4y t4z t4| t4} t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t4 t5 t5 t5 t5 t5 t5 t5 t5 t5 t5 t6 t6 t6 t6 t6 t6  t6  t6 t6 t6 t6 t6 t6 t6 t6 t6  t6! t6" t6' t6( t6* t6/ t61 t65 t68 t6= t6= t6+ThatE6-y60y61y63y64y65y68y6:y6<y6=y6?y6@y6Ay6By6Cy6Dy6Ey6Gy6Hy6Iy6Jy6Ky6Ly6My6Ny6Oy6Py6Qy6Ry6Sy6Ty6Uy6Wy6Xy6Zy6]y6^y6_y6`y6ay6by6ey6fy6gy6iy6jy6my6py6sy6ty6uy6vy6wy6xy6yy6zy6{y6|y6}y6}y6}y6}y7magneticyta2a&aZa)aaaa aalaaa"ya&a)(a)a+~a+a+a+a-a,a+a6a6Ta6[a6]a6ga6ua6{a6a6a6a7a7La7^a7qa7va7a7a7a82a8;a8na8a8a8a4X'a7'a7'a8'aallyz z*% z6Ys8r z8y z&zationh h h  i i'^ iZ i; i i!= i8q i  i  i i i  i$ i ir i  i$U i6 i6 s82 s8q s8y s8 s8 s8 s6s6s44Uids34;P4HP4GP4FP4EP4DP4CP4?P4AP4@P4>P4<P41P4IP4UP4MP4NP4OP4PP4QP4RP4SP4TP4VP4WP4]P4\P4[P4ZP4YP4XP4gP4fP4eP4dP4cP4bP4aP4`P4_P4^P4nP4mP4lP4kP4jP4iP49P4)P4P4P4P4P4P4P4P4P4P4P4P4P4PgrowthEPPPP(P?PWPPPPP"P$P.P'3P'8PPPPPPPPPPPPPP OP P ^P >P QP P P P PPPP+PP"P$P[PZPPP PqPPPPPPP<PGPPP.P4YEnTRezp4Xo4go4fo4eo4do4co4bo4ao4`o4_o4^o4no4mo4lo4ko4jo4io49o12o4)o4o4o4o4o4o4o4o4o4o4o4o4o4o4o4o4o1o3io/o1o1o2o2o20o1o/o2Wo2o4:o5:o5<o5;o5=o5Co5Do5Eo5Go5Fo5Io5Ho5HoH5o'ZOfc%@N%QN%hN%pN4N'AN%DN4N4N4N5N2WNN+N<N2N5 NN5N5N(N51N54N55N3N58N59N/N5:N5=N5>N5?N5AN5BN5DN5GN5FN5IN5HN5KN5JN5MN5LN5PN5ON5NN5QN5RN5SN5UN5TN5VN5]N5\N5\N5\N5\N5\N\5N\5N\5N\5N\5NRajappa, S.` 1991d]ALAMETHICIN AMINO-ACID SYNTHESIS ASYMMETRIC-SYNTHESIS CONFORMATION DERIVATIVES PROTEINS UNITS~Nitroacetyl Group As a Peptide Synthon - Synthesis of Dipeptides with an alpha,alpha-Bisallylglycine Residue at the N-TerminusHelvetica Chimica Acta745 1071-1080 48062+Manly, S.P. Matthews, K.S. Sturtevant, J.M.e 1985@9Thermal denaturation of the core protein of lac repressor Biochemistry2415 3842-3846 16 Jul( INvestigation v v v v v v? vd v vd v v& v* v  v) v5 v v v1 v v v) vW v vG v v v 4 v  v# v# v&| v+ vd v, v v/ v. v3 v3 v4 v7q vF v  vB v s: s s 7 s s( s% s+p s6 s6x s7H s7q s7 s8o s sv [v \v vvvzvyv{vvv"v/Mv3v5v5v6v Wvv |vvvkv}v8)v8v8v veM  M  M MMENTi4?isible#tesAroBos sv [v \v vvvzvyv{vvv Wvv |vvkv}v veM  M  M MMENTiAitroBoooPer#^a#a+|a+a0a6-a6Ca6ja6}a6a6a7a7a8oa8za8a46'a%ahiakkylaltacc6/kylcent#aaa xage"M p8F p7ptron  sGhlorateicaivals smithyOLL y E zel D Ddd dd!d$d#d"d'd&d%dd deuteratedEZ E. E4 E8y E * E Ez E| E8 i& ion6w8aw(wEGRINAi)ira3ddasilva*llo#`r*rat-iam(tz^ZzZz E zel D Ddd dd!d$d#d"d'd&d%dd deuteratedEZ E * E Ez E| E& ion(wEGRINAi)iradasilva*llo#`r*rat(tzmZzzZ CerEvisiae i S   I F *i |   T  a     S E! E  E< EJ y l  5 sT   Z|         I  O6 V  v  A  k  !# ! "6 # # #A #n $ $ %  !1y !2 J2 y4 7 5J TZ  i S   I F *i |   T  a     S E! E  E< EJ y l  5 sT   Z|         I  O6 V  v  A  k  !# ! "6 # # #A #n $ $ %  !1y !2 J2 y4 7 5J T JAH2an2bn.JnLn2dn2cn2en2fn2gn2in2hn2jn0~n2nn2mn0n n2onn2pn2qn tn2nen2n2n2n2n2n2n2n2n,n3n3n3n3n3'n3(n3)n3*n3+n3,n3-n3.n3/n30n31n32n33n34n35n36n3:n39n38n37n3@n3;n3<n3=n3=n3=nWaltern h h h h h hsZs.s^s_sss*5s)$ss)s)s&s s s"s#s#s$s$s%+s&s&s+Js+cs+ds)EsIsHs&ss#s1 ss1s0s*ss&s@s=s0s1*s)Fs s1"s1,s2s2s2s2s2s2s2s2s10494$3&?303o30380983:36:5856:939382815283f63f8683687f70327f8855555500 0 0 0 00000C0000Y0B00!M0!0"0+0(0#01_0-02e0506506600 000 0 2010$000L08$09709G00_0+0n02e0 a0b41V411Fullt1b1b1b1b1b1b1b1b2b2b2b2b2b/b2b2 b24b2<b2Lb2]b2ab2bb2db2eb2gb2ib2nb2rb2sb2vb2b2b2b2b2b2b2b2b2b2b2b2b2b2b2b2b2b1Vb2b2b2b2b2b2b2b2b2b1>b2b2b2b2b 02115, USA3Journal of Bacteriology 5097.'Michalak, K. Gutowicz, J. Modrzycka, T. 1992CELL MEMBRANE ENZYME-LIPID INTERACTION ERYTHROCYTE-MEMBRANE FLUORESCENCE QUENCHING FLUORESCENT PROBE GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE LIPID VESICLES PHOSPHATIDYLINOSITOL LIPOSOMES PROTEINSxqTemperature Studies of Glyceraldehyde-3-Phosphate Dehydrogenase Binding to Liposomes Using Fluorescence Techniquei(!General Physiology and Biophysicsd116545-554i DeccB Rodseth1992! Roe19932 Roe19972 Roe1997 Roebber1992 Roebber1992- Roepstorff1999 Roger1992g Rogero19801.z Rogero19859+ Rogers19649 Rogers19911 Rogers19911 Rogers19922 Rogers1992 2 Rogers2000  Roggenkamp1992 F Rogl19969 Rognan1992  Rogov1991 Rogov1992.Rogowski1999-4Rogowski20030( Rohde1987< Rohde1993 Rohde1994 Roher19934 Roher2002 Rohl1992v Rohl1994v Rohl1995v Rohl1996v2 Rohl20024 Rohl200208~ Rohl200228I Rohl20030 Rohlf19817 Rohlk1993 Rohr1992 Rohren1993  Rohrer1990  Rohrer1993 s Roig19616 Roise1992!! Roise1992 Roise19935Roitberg2002Z Rojas1993 Rojas1993 Rojo1991 Rojo1993v K Rojodominguez1993  Rojodominguez1993- Rokhlin19976 Rokhsar1998"d Rokop1990 Rollema1993# Rollema19937 Roller19929K Roller1993M Roller1993 L Roller1993 Rolles19888 Rolles19899# Rollo1988 Rollo1988r Rolls1993)# Rolls1998. Romagnoli1999 Roman1992% Roman1993 Roman1993+ Roman19980+ Roman1999"f Romano19922 Romano19933 Romano1993  Romanowski1992 ^ Rome19919 Romeo1993 Romer1993.C Romero1999g Romi19931 Romier1993 7 Romisch1990* Romisch1997 Rommelaere1993  Romoff19922 Ron19932 Ron20002 Ron20004 Ron2002m Ronchi199197 Rondahl1992 Rong1993v? Rong19959! Ronne1985 Ronne1993 Ronni199258 Ronning2003 Roobol1993  Rook1992v* Rook19989 ) Rooke1991* Rooman1988  Rooman1991  Rooman1992 Rooman1992 +* Rooman19989 Roomans1992 L Rooney1993n Roonprapunt1992 Roop1992v0 Roos199190 Roos199917 Roos2001h Roosendaal1991 Root19939 Roper1992 Ropp19933 Ropson19909 Ropson1990 & Ropson1991 Ropson1992  Ropson19939( Ropson1997 ++ Ropson19989, Ropson19989/ Ropson20006 Ropson200002 Ropson2001<2 Ropson2001 Roques1989u ) Roques19911& Roques1992n Roques1993s Roques19939+ Roques19939 Rorschach1990 Rorschach1992 Rorsman1991} Ros1992o Rosa19919 Rosato1992 Rosato19933#m Rosch1990/M Rosch1990*u Rosch1994,Q Rosch1997 < Rose1975) Rose1985v& Rose1986k Rose19888 Rose1990 Rose19919/ Rose1992v Rose19921 Rose19922 Rose19929 Rose19929 Rose19939k Rose1993v Rose19939 Rose19939 Rose19931z Rose19939u Rose19933 Rose1993v Rose19944 Rose1994n U Rose1995n* Rose1997n* Rose1997v* Rose1997n4 Rose1997n* Rose19989* Rose19989, Rose199896p Rose19989.^ Rose19999._ Rose199992 Rose20006w Rose200006 Rose2000n6 Rose20005 Rose2003364 Rose2003n8L Rose20032NRosejohn199114 Roseman1975h Roseman1991 Roseman1991 Roseman1992 Roseman1993 Roseman1994-d Roseman1996 Rosen1988B Rosen1991 Rosen1992^ Rosen1992T Rosen1992% Rosen1992 Rosen1992% Rosen1993% Rosen1993) Rosen1993# Rosen19932 Rosen1997/ Rosen1999. Rosenbaum1999= Rosenberg1975 c Rosenberg1981  Rosenberg1982  Rosenberg1989  Rosenberg1990  Rosenberg1990! Rosenberg1991 Rosenberg1992$@ Rosenberg1992 Rosenberg19928 Rosenberg1992F Rosenberg1993q Rosenberg1993 Y Rosenberg1993 Rosenberg1993 Rosenberg1993-` Rosenberg1993 Rosenberger1993-K Rosenberger1994? Rosenberger1995- Rosenblatt1987f Rosenblatt1991  Rosenblatt1993  Rosenblum1996 Rosenbusch1990  Rosenbusch1991  Rosenbusch1992 8*Rosendal2003o Rosenfeld1991 Rosenfeld1992 Rosenfeld1992 Rosenfeld1992 Rosenfeld1992 Rohrer1993 s Roig19616 Roise1992!! Roise1992 Roise1993Z Rojas1993 Rojas1993 Rojo1991 Rojo1993v K Rojodominguez1993  Rojodominguez1993- Rokhlin1997) Rokhsar1998"d Rokop1990 Rollema1993# Rollema19937 Roller19929K Roller1993M Roller1993 L Roller1993 Rolles19888 Rolles19899# Rollo1988 Rollo1988r Rolls1993)# Rolls1998. Romagnoli1999 Roman1992% Roman1993 Roman1993+ Roman19980+ Roman1999"f Romano19922 Romano19933 Romano1993  Romanowski1992 ^ Rome19919 Romeo1993 Romer1993.C Romero1999g Romi19931 Romier1993 7 Romisch1990* Romisch1997 Rommelaere1993  Romoff19922 Ron1993m Ronchi19919 Rong1993v? Rong19959! Ronne1985 Ronne1993 Ronni1992 Roobol1993  Rook1992v* Rook19989 ) Rooke1991* Rooman1988  Rooman1991  Rooman1992 Rooman1992 +* Rooman19989 Roomans1992 L Rooney1993n Roonprapunt1992 Roop1992v0 Roos19919h Roosendaal1991 Root19939 Roper1992 Ropp19933 Ropson19909 Ropson1990 & Ropson1991 Ropson1992  Ropson19939( Ropson1997 ++ Ropson19989, Ropson19989/V Ropson20000/ Ropson2000 Roques1989u ) Roques19911& Roques1992n Roques1993s Roques19939+ Roques19939 Rorschach1990 Rorschach1992 Rorsman1991} Ros1992o Rosa19919 Rosato1992 Rosato19933#m Rosch1990/M Rosch1990*u Rosch1994,Q Rosch1997 < Rose1975) Rose1985v& Rose1986k Rose19888 Rose1990 Rose19919/ Rose1992v Rose19921 Rose19922 Rose19929 Rose19929 Rose19939k Rose1993v Rose19939 Rose19939 Rose19931z Rose19939u Rose19933 Rose1993v Rose19944 Rose1994n U Rose1995n* Rose1997n* Rose1997v* Rose1997n* Rose19989* Rose19989, Rose19989.^ Rose19999._ Rose19999NRosejohn19911h Roseman1991 Roseman1991 Roseman1992 Roseman1993 Roseman1994-d Roseman1996 Rosen1988B Rosen1991 Rosen1992^ Rosen1992T Rosen1992% Rosen1992 Rosen1992% Rosen1993% Rosen1993) Rosen1993# Rosen1993/ Rosen1999. Rosenbaum1999= Rosenberg1975 c Rosenberg1981  Rosenberg1982  Rosenberg1989  Rosenberg1990  Rosenberg1990! Rosenberg1991 Rosenberg1992$@ Rosenberg1992 Rosenberg1992F Rosenberg1993q Rosenberg1993 Y Rosenberg1993 Rosenberg1993 Rosenberg1993-` Rosenberg1993 Rosenberger1993-K Rosenberger1994? Rosenberger1995- Rosenblatt1987f Rosenblatt1991  Rosenblatt1993  Rosenblum1996 Rosenbusch1990  Rosenbusch1991  Rosenbusch1992  Rosenfeld1991 Rosenfeld19921992&3 0)0 0 O0 0 0_060e000X00M000X0000)0p0000000'00000 0}000%0v000$0X00000l00#0_0o0~000C0d00 N0 Y0 0 0!'0N TEmperature s s s s s_ s s s s s s s s s s s s s s s f s  s  s  s' s  s  s  s  s  s  s s\ s s s st s sn s s s s s s s  s sv s s s sF s s s% s) s} s s s s7 s s#z97169)*94264)44w7688374)8'S84164a25.40+^04156+^369576872526648#z37+5027w4+j2439+j8)-86775n5"6723109767849689499))69079),77171n96044453100680683222 2%:2,C2{00e00+h04381+h2+i2+i22)1231756449+e3398)+e4).40875)+597934M'02'16'47c'46412144674703)58221)63)G70073+k3813F+k7+l7+l7+f70148+f83iQUery1s1s2s2s20s1s2Ws2s4:s5:s5<s5;s5=s5Cs5Ds5Es5Gs5Fs5Is5Hs5Ks5Js5Ms5Ls5Ps5Os5Ns5Us5Ts5Ys5Xs5Ws5Vs5]s5\s5[s5Zs5^s5ds5cs5bs5as5`s5_s5ls5ks5js5is5hs5gs5fs5ms5qs5ps5os5ss5rs5zs5ys5xs5ws5wsIBULOSE BISPHOSPHATE CARBOXYLASE{A Novel ATPase Complex Selectively Accumulated upon Heat Shock Is a Major Cellular Component of Thermophilic Archaebacteriao EMBO Journal107 1711-1722 JulD 6136 Phoenix, D.A. Pratt, J.M.P 1990&DOMAIN MEMBRANE SURFACE PROTEIN tmPH-Induced Insertion of the Amphiphilic Alpha-Helical Anchor of Escherichia-Coli Penicillin-Binding Protein-5N& European Journal of Biochemistry 1902 365-369P 20 JunrARchersi'[iiii'Ci9tt3,t0typei1 i iN itectural. e4 e eN e e v v$_ v* v+ v6+ v7 v7_ v v D vc v) v4 v  s6G s6f s6 s7: s7p s7 s8H s8 s8 s/U sN v6 v v e- alu-es6u}uu2i'7ifiiiii*iiCi {i i i i i i i i i yiiiEiEiEi6Similar6i6i6i6i6i6i6i6i6i6i6i7-i7Ai7oi7pi7qi7i7i7i7i8i8!i8di8pi8i8i8i8i8i8i8i8i8i8i8i6i8iities yV y y k y  y"L y#p y/ y4g y5B y y y y y y y y y'J y+ y6 y7 y/ y p p p p p p p pi6i6i6i6i7-i7Ai7oi7pi7qi7i7i7i7i7i7i8i8!i8di8pi8i8i8i8i8i8iities yV y y k y  y"L y#p y/ y4g y5B y5 y y y y y y y y y'J y+ y6 y7 y7 y/ y p p p p"Exchangei#l#l#l#l#l)l$yl$l$l%l&l%<l%=l%_l)l%l&l&Bl&Pl(l+Ql)3l Sl+l+l'`l,l l&l&Sl&l&l)lbl,l,l-lll(ltl(ll+l[l->l-Nl!l=l-l-l-l.+l.-l.2l.3l.>l.ml.yl.yl.yly.ly.l6*431 x 5fbacteria. The low molecular weight d,l-alpha-peptides offer an attractive complement to the current arsenal of naturally derived antibiotics, and hold considerable potential in combating a variety of existing and emerging infectious diseases.'~Present address: Departamento de Quimica Organica, Universidad de Santiago de Compostela, 15706 Santiago de Co12581663131 2003 Feb&Early events in protein folding 75-81'XRMRC Centre for Protein Engineering, MRC Centre, Hills Road, CB2 2QH, Cambridge, UK Ferguson, N. Fersht, A. R.Curr Opin Struct Biolclehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12581663h 216282Fernandez, J. Demott, M. Atherton, D. Mische, S.M. 1992CLEAVAGE PEPTIDE POLYACRYLAMIDE GEL ELECTROPHORESIS PREPARATIVE ELUTION PVDF MEMBRANES SEPARATION STRATEGIES TWO-DIMENSIONAL GELScInternal Protein Sequence Analysis - Enzymatic Digestion for Less Than 10 mug of Protein Bound to Polyvinylidene Difluoride or Nitrocellulose MembranesdAnalytical Biochemistry 2012255-264 MarVPFernandez, E. Bienvenu, T. Arramond, F.D. Beldjord, K. Kaplan, J.C. Beldjord, C. 1993Use of Chemical Clamps in Denaturing Gradient Gel Electrophoresis - Application in the Detection of the Most Frequent Mediterranean beta-Thalassemic Mutations"PCR Methods and Applications32122-124d Oct 2161DNA SINGLE-BASE CHANGES Fernandez, A. 2002VOTime-resolved backbone desolvation and mutational hot spots in folding proteinsiProteins474i447-57.w12001223 JAHZShttp://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?db=m&form=6&dopt=r&uid=12001223wTNFernandez, A. Shen, M. Y. Colubri, A. Sosnick, T. R. Berry, R. S. Freed, K. F. 2003>8Large-scale context in protein folding: villin headpiece Biochemistry423n664-671m Jan 2812534278 JAH lehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12534278r'nhInstitute for Biophysical Dynamics, James Franck Institute and Department of Chemistry, and Department of Biochemistry and Molecular Biology, University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, and Instituto de Matematica, Universidad Nacional del Sur, Consejo Nacional de Investigaciones Cientificas y Tecnicas, Bahia Blanca 8000, Argentina.12518060 100o1v 2003 Jan 7rVPInsufficiently dehydrated hydrogen bonds as determinants of protein interactions 113-8ld]The prediction of binding sites and the understanding of interfaces associated with protein complexation remains an open problem in molecular biophysics. This work shows that a crucial factor in predicting and rationalizing protein-protein interfaces can be inferred by assessing the extent of intramolecular desolvation of backbone hydrogen bonds in monomeric structures. Our statistical analysis of native structures shows that, in the majority of soluble proteins, most backbone hydrogen bonds are thoroughly wrapped intramolecularly by nonpolar groups except for a few ones. These latter underwrapped hydrogen bonds may be dramatically stabilized by removal of water. This fact implies that packing defects are "sticky" in a way that decisively contributes to determining the binding sites for proteins, as an examination of numerous complexes demonstrates.s'PIInstitute for Biophysical Dynamics, University of Chicago, IL 60637, USA.s$Fernandez, A. Scheraga, H. A.d("22406340 0027-8424 Journal ArticleProc Natl Acad Sci U S ADesiccation/*methods Dimerization Hemoglobins/*chemistry Human Hydrogen Bonding Models, Molecular Protein Conformation Protein Subunits/chemistry Proteins/*chemistry/metabolism Support, U.S. Gov't, Non-P.H.S.lehttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=12518060 4 D .(Journal of the American Chemical Society 121 10119-10125  SJE 4122Kroh, H.E. Simon, L.D. 1991~wCOMPONENT DEGRADATION EXPRESSION FACTOR SIGMA 32 HEAT-SHOCK PROTEIN HIGH-TEMPERATURE HTRA GENE ION-GENE MUTANTS PRODUCTMvoIncreased ATP-Dependent Proteolytic Activity in Lon-Deficient Escherichia-Coli Strains Lacking the DnaK ProteineJournal of Bacteriologye 1738r 2691-2695( Aprf(808Y08a08f08q08080808060/0/0/0/0/0/0/0/0/0/04)05060707070-z0-0504060704W'07'0^0(6!76#_6#6,646$6B6(66-662x2I222)2!D0!00=04)06'060608,0 d02{1576816'2260/0/0/0/0/0/0/0/0/0/04)05060707070-z0-0504060704W'07'0^0(6!76#_6#6,646$6B6(66-662x2I222)2!D0!00=04)06'060608,0 d02{1576816'226Enzymenss 0s Ds Xs s #s s s )s%s7ssssssss\ssssshsss`s*s+s4sssss)ss(s*ss*smsnssos/ssssss!ssssss*s4s\ssCs|toolrss!s&Ps*xs%s/s1s36s4e5e6e8<eje6e6e6e6&e7He7Ie7e8<e8oe8e8e2es!p)z"UT/ T0n19n6n7Kn<n)n)'n6(n6n6n8Gn8nn THz=zeg"Ap pp-Fi/h!Dh+wh8,h8Ih"Bham7icssoo \o$ogeenesisr r6 i i!* I!+ I0 I6P I7 IICr  r r8w rLraphica a8 a aly y y " I$ I I I  I  I  IWevaaaa)$a%aQa)a$a'aaaaaa*aaaa%a^aoaaaaaCa)a)a&aaa _a a a!a!a!a"Ca"Ea"Ma)a# a#/a#qa#{a$Ua$a%a&/a&0a&a)a)(a)+a),a)-a)1a))a+Xa+[a+^a+ea14T1Fa1Ka1Ma1Qa1Sa1]a1^a1ia1ka1oa1pa1qa1sa1ta1ua1va1wa1xa1a1a1a1a1a1a1a1a1a1a1a1a1aa1a1a1a1a1a1a1a/a2a2a2 a2a2a2+a2.aa/a23a*a24a25a2Ca2Da2Ea2Na2Ma2Oa2Oa2Oa2Oa2Oaorigins8R>ii-mi-ii4i5Li%.i6(i7qi7ii&R6Nnetation5'on$P1 RT ladonpndnB eansi2v'o5'o5'o6I'oovn6a+ynithines g s  su s" s-` s6@ s s s  s V s s sE sA s s s s!l s!~ s! s$ s+y s6@ s6 s6 s g s s6@ s6 s6 sstein& opeza haryngeal x$Jszlan1zco/zphany61r. rayoonrrt+Yu3'S7'aygtegontegonang1993 Huang1993 Huang1993Houghten19922"Houghten1992Houghten19922Houghten19922 Houghten1993Houghten19933Houghten19955(Houghten19979)Houghton1984)Houghton1985- Hoult1990[Hounslow1993`Hounslow1994=/ Unfolding/ r/ r/ r/ r/ r/ r0 r/ r r0 r.4 r0- r0. r0 r0 r0 r0 r0 r0 r" r1 r r r1 r1 r1 r1 r1 r1 r1 r. ru r2 r r23 r2B r2C r2c r2i r2| r3 r3 r3, r3? r3B r3I r2 r3W r3u r3x r3p r3z r3 r3 r3 r3 r3 r3 r3 r4 r4  r4  rRNAseDe e zeeee eeLeeAe e e%Ie)e)e^e)e :e 9e)e)e)e)6e)5e)-e)*e6e6e7e*ejodoo*o{o~ooo o,o,oo.o/qouo2Mo8o1ooPdPPbPP PPPC)C6 s6:s6s6s8s8s8fs8s-sC7_P7ms8Hs7_s7mP+pP)1)$1+g1crobiological Reviews49359-378Booth, D.R. Sunde, M. Bellotti, V. Robinson, C.V. Hutchinson, W.L. Fraser, P.E. Hawkins, P.N. Dobson, C.M. Radford, S.E. Blake, C.C.F. Pepys, M.B. 1997leInstability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.@ Nature 385d787-793 SJEBooth, P.J. Curran, A.R. 1999 Membrane protein folding.,%Current Opinion in Structural Biology9115-121  SJEd9876$4532 3991voKnegtel, R.M.A. Katahira, M. Schilthuis, J.G. Bonvin, A.M.J.J. Boelens, R. Eib, D. Vandersaag, P.T. Kaptein, R.  1993AMINO-ACIDS DISTANCE GEOMETRY DNA-BINDING DOMAIN ESTROGEN-RECEPTOR GLUCOCORTICOID RECEPTOR HEPATOCELLULAR-CARCINOMA IDENTIFICATION NMR-SPECTROSCOPY NUCLEAR MAGNETIC-RESONANCE RESPONSIVE ELEMENT RETINOIC ACID RECEPTOR SOLUTION STRUCTURE THYROID-HORMONE ZINC FINGERThe three-dimensional structure of the DNA-binding domain of the human retinoic acid receptor-beta (hRAR-beta) has been determined by nuclear magnetic resonance spectroscopy in conjunction with distance geometry, restrained molecular dynamics and iterative relaxation matrix calculations. A total of 1244 distance restraints were obtained from NOE intensities, of which 448 were intra-residue and 796 inter-residue restraints. In addition 23 chi and 30 phi dihedral angle restraints were obtained from J-coupling data. The two 'zinc-finger' regions of the 80-amino acid residue protein are followed by two alpha-helices that cross each other perpendicularly. There is a short stretch of b-sheet near the N-terminus. The alpha-helical core of the protein is well determined with a backbone root-mean-square deviation (r.m.s.d.) with respect to the average of 0. 18 angstrom and 0.37 angstrom when the side chains of residues 31, 32, 36, 61, 62, 65 and 69 are included. The r.m.s.d. for the backbone of residues 5-80 is 0.76 angstrom. For the first finger (residues 8-28), the r.m.s.d. of the backbone is 0.79 angstrom. For the second finger (residues 44-62) the r.m.s.d. is 0.64 angstrom. The overall structure is similar to that of the corresponding domain of the glucocorticoid receptor, although the C-terminal part of the protein is different. The second alpha-helix is two residues shorter and is followed by a well-defined region of extended backbone structure.XRThe Solution Structure of the Human Retinoic Acid Receptor-beta DNA-Binding Domain"Journal of Biomolecular NMRN3O1 1-17 Jan  3995Knight, K.L. Sauer, R.T. 1988tnThe Mnt repressor of bacteriophage P22: role of C-terminal residues in operator binding and tetramer formation Biochemistry276` 2088-2094P 22 Mar 3996Knight, K.L. Sauer, R.T. 1989f`Identification of functionally important residues in the DNA binding region of the mnt repressor&Journal of Biological Chemistryi 26423 13706-13710 15 Aug 3994F?Knight, K.L. Bowie, J.U. Vershon, A.K. Kelley, R.D. Sauer, R.T.u 1989VPThe Arc and Mnt repressors. A new class of sequence-specific DNA-binding protein&Journal of Biological Chemistry  2647D 3639-3642S 5 Mar 3997Knight, K.L. Sauer, R.T. 1989rlDNA binding specificity of the Arc and Mnt repressors is determined by a short region of N-terminal residues863A797-801 FebVOProceedings of the National Academy of Sciences of the United States of America 3992,&Knight, C.A. Cheng, C.C. Devries, A.L. 19912,GLYCOPEPTIDES GROWTH INHIBITION POLAR FISHES\VAdsorption of alpha-Helical Antifreeze Peptides on Specific Ice Crystal Surface PlanesBiophysical JournalO592M409-418I Feb 3998Knight, K.L. Sauer, R.T. 1992ARC REPRESSOR BACTERIOPHAGE-P22 COLI RNA-POLYMERASE LAC REPRESSOR METHYLATION INTERFERENCE OPERATOR MUTANTS PROTEIN DNA CONTACTS PROTEIN MUTANTS PROTEINS RECOGNITION REGION RESOLUTION SPECIFICITY SYMMETRY TERMINAL RESIDUESBiochemical and Genetic Analysis of Operator Contacts Made by Residues Within the beta-Sheet DNA Binding Motif of Mnt Repressor0 EMBO Journal111n215-223 Jan 3993*#Knight, J.S. Madueno, F. Gray, J.C. 1993AMINO-ACID SEQUENCE ENVELOPE POLYPEPTIDE HEAT-SHOCK PROTEIN NUCLEOTIDE-SEQUENCE PEA-CHLOROPLASTS PHOSPHATE TRANSLOCATOR PRECURSOR PROTEIN SPINACH-CHLOROPLASTS THYLAKOID MEMBRANES TRANSIT PEPTIDE4.Import and Sorting of Proteins by Chloroplasts& Biochemical Society Transactions211 31-36P Feb8lethalttkttt t$St+[tt5t6=t1tatiiii#i [i!i"vi$&ioi0i6+i6=i6fi6pi7aiity t t tc o o o+[ o5 o7' ooffeu#u urneurt  t+|t0e1e1<e1Le1e2e2e2e3Le5e5e6e6e6e7e7e7e75e7@e7Ee7ee7ze7e7e7e7e8e8e8e8e9e9e90e95e96eze4ee+|eerssWss*sity t t tc o o o[+ o5 ooffeu#u urneurt  t|+t0e1e<1eL1e1e2e2e2eL3e5e5e6eze4ee|+eerssWss*sse+p+p%%+'"%+Y2++'d+ f]s+ AF)&*rn!Fn+4,6* (m,@,$'9,Sl,a,f,h'Pb+^'P ,&%,-,,'R"-,, l+V$$,,,v( ,"- +3vo1bdR)(HA"Dg}cd,) oj-q---{-(c6\diH,@e~'UD5!?'UYmy/1&'U-&&$L>G,f,fZ*=/-J^ w Kovats19909 Kover19926 Kowal1994 Kowalczyk1993  Kowalczyk1993- Kowalewski1999 Kowall1991 nKowalski1992Kowalski19939; Kowarik2002 Koyama1993 " Koyama19939 Kozak1989 Kozak1991 Kozak1992\ Kozasa1991  Kozhich1993 Kozhich19930y Kozin2001 Kozlov1993 1 Kozlov20022. Kozlovskaya1999% Kozlowski1992 Kozlowski1992! Kozlowski1992 Kozma1993 & Kozytch1992+( Kvr1998 Kraal1993 Kraayenhof1993 6+ Kraehenbuehl20010  Kraehenbuhl1993) Kraemer1995( Kraft1987' Kraft1990 Kraft1992 Kraft1993 Kragelund1993+ Kragelund1995 Kragelund1996'Q Kragelund19966 Kragelund1996, Kragelund1998- Kragelund1999- Kragelund19992? Kragelund20003h Kragelund20023 Kragelund20022 Kragol2001 8R Kragol2002 Krajcarski1993 ? Krajewski1987x Krajewski19882 Krajewski1995>Kralicek1992Kralicek1993 Kramer19911 Kramer19929 Kramer1993  Kramer19933#5 Kramer19939" Kramer199397 Kramer199599? Kramer199772 Kramer199887 Kramer1998-7 Kramer199991f Kramer200101i Kramer200117% Kramer20017& Kramer200149 Kramer20024 Kramer20027' Kramer200275 Kramer2002a5 Kramer2003c Kranold1992/b Krantz2000 1 Krantz2000<1 Krantz2002<3; Krantz2002<U Krapp1992" Krasheninnikov1982gKrasheninnikov19937Krasheninnikov1997&% Kratz1992 Kratzer1991 Kraulis1987 Kraulis1988 Kraulis1989 Kraulis19916 Kraulis19912 Krause1982+g Krause19878 Krause1993 Krause19969  Krauss1984 ) Krausz1991 Z Krausz19929 Krausz1992 Kraut1991Z Kraut1991Y Kraut1991\ Kraut1991[ Kraut19918 Kraut1991. Krauth-Siegel1997 Krchnak1993. Krebber1993/ Krebs1983 V Krebs1991 c Krebs1993 Krebs1993 Krebs1993 Krebs1993  Krebs19930 Krebs2000\ Kreft19915 Kregel2002%Kreibich1990Kreibich1995- Kreienkamp1992 Kreil1987t Kreis1990 Kreis1992 Kreis1992 Kreis1993 Kreizman1993' Krejchi1994 Krejchi1994 Krekel199494< Kremer20022 Krengel1990> Kresge19922 Kress1993% Kretsinger1991 J Kretsinger1991  Kretsinger1992  Kretsinger1992  Kretzschmar1993 Kreusch19918T Kreutzenbeck2003P Krezel1991  Krieg1986 Krieg1989 Krieg1990 Krieger19935 Krieger20036U Kriegl2003a Krimm1990  Krimm1991z Krimm1992| Krimm19932 Krimmer2000 Krin19939 Krinks1990  Krinks1990  Krinks19911 Krinks1991 Krischer1989 Krishna19924 Krishna1993c Krishna19930 Krishna200144 Krishna2002Krishnamoorthi1992#Krishnamoorthi1993.7Krishnamoorthy1999"1Krishnamoorthy2000;0Krishnamoorthy2001Krishnan1991-Krishnan1997/Krishnan20003# Krishnasastry1992 Kristensen1992 - Kristensen19991 Kristensen20028 Kristensen2003- Kristiansen1999- Kristiansen1999Kriwacki1993.Kriwacki19960Kriwacki200221 Kroczynska2001Q/ Kroenke1999/ Kroenke2000/ Kroenke20006 Kroenke2000 Kroes1992 Kroh1991v2 Krojer2002 Krol199396 Krolikowski1999- Kroll1999 Kromer1992  Kromminga1993. Kromminga1994"X Kron1987 Kronidou1993 ? Kronke19933 Kronman1992 Kronman1993 Kroon1993#) Kroon19931 Kroon20015 Kroon2003Kroonbatenburg1992 Kropshofer1991  Kropshofer1992 Kropshofer1993 Krovatin1983 Krska1992 Krska1993 Krstenansky1991 Krstenansky1991/ Kruber19989 Krudy1992 Krueger19928 Krueger1999 Krug19922f Kruger1992 / Kruger20000 Krugh1993 Krull1992 Krupenko1991_ Kruppa19969-P Kruppa2000 Kruse1993. Kruse1999Krushelnitskii19920\ Krust1997NKruttgen19911) Krylov199553 Kryndushkin2002 Krystek1992 Krystek1992 Krystek19939_ Krystek20051cKrzewska2001 Ksenzenko1993 Ksiezakreding1991 Ksiezakreding1992 Ktistakis1990 Ktistakis1992 Ktistakis1992 Ku19939*0 Kuang1997* Kuang1998.) Kuang19995? Kubelka2003 Kubica1992a"L Kubicek1993 Kubina19929 Kubo19933 Kubo1993v Kubo1993v/ Kubo200002 Kubo200009[ Kubo20020# Kubota1991  Kubota1991  Kubota1992  Kubrich1993 Kuby1991v!Kuchinka19939 Kuciel19939'P Kuczer19969- Kuczera2004U Kudinov1983V Kudinov1984Kudlicki1992"Kudlicki199337Kudlicki19959?Kudlicki1997l7Kudlicki19980N Kudo1991 Kuehn1991 Kuehn1992 Krebs1993  Krebs1993\ Kreft1991%Kreibich1990Kreibich1995- Kreienkamp1992 Kreil1987t Kreis1990 Kreis1992 Kreis1992 Kreis1993 Kreizman1993' Krejchi1994 Krejchi1994 Krekel19949 Krengel1990> Kresge19922 Kress1993% Kretsinger1991 J Kretsinger1991  Kretsinger1992  Kretsinger1992  Kretzschmar1993 Kreusch1991 Krezel1991  Krieg1986 Krieg1989 Krieg1990 Krieger1993a Krimm1990  Krimm1991z Krimm1992| Krimm1993 Krin19939 Krinks1990  Krinks1990  Krinks19911 Krinks1991 Krischer1989 Krishna19924 Krishna1993c Krishna1993Krishnamoorthi1992#Krishnamoorthi1993Krishnan1991-Krishnan1997# Krishnasastry1992 Kristensen1992 - Kristensen1999- Kristiansen1999- Kristiansen1999Kriwacki1993 Kroes1992 Kroh1991v Krol19939- Kroll1999 Kromer1992  Kromminga1993"X Kron1987 Kronidou1993 ? Kronke19933 Kronman1992 Kronman1993 Kroon1993#) Kroon1993Kroonbatenburg1992 Kropshofer1991  Kropshofer1992 Kropshofer1993 Krovatin1983 Krska1992 Krska1993 Krstenansky1991 Krstenansky1991 Krudy1992 Krueger1992 Krug19922f Kruger1992  Krugh1993 Krull1992 Krupenko1991_ Kruppa19969-P Kruppa1999 Kruse1993Krushelnitskii1992NKruttgen19911) Krylov19955 Krystek1992 Krystek1992 Krystek1993 Ksenzenko1993 Ksiezakreding1991 Ksiezakreding1992 Ktistakis1990 Ktistakis1992 Ktistakis1992 Ku19939*0 Kuang1997* Kuang1998.) Kuang1999 Kubica1992a"L Kubicek1993 Kubina19929 Kubo19933 Kubo1993v Kubo1993v# Kubota1991  Kubota1991  Kubota1992  Kubrich1993 Kuby1991v!Kuchinka19939 Kuciel19939'P Kuczer1996U Kudinov1983V Kudinov1984Kudlicki1992"Kudlicki19933 Kuehn1991 Kuehn1992 r45?@T 4133& Ksenzenko, S.M. Brusilow, W.S.A. 1993>8ATP SYNTHASE CHANNEL CLONED GENES EXPRESSION F1F0 ATPASE|Protein Lipid Interactions of the Proteolipid-c Subunit of the Escherichia-coli Proton-Translocating Adenosinetriphosphatase.'Archives of Biochemistry and BiophysicsY 305I1 78-83 15 Aug 4134,%Ksiezakreding, H. Liu, W.K. Yen, S.H. 19922,ABNORMAL PHOSPHORYLATION ALKALINE-PHOSPHATASE ALZHEIMER NEUROFIBRILLARY TANGLES ALZHEIMER-DISEASE ANTIGENIC DETERMINANTS DEPENDENT KINASE DISEASE BRAINS GEL-ELECTROPHORESIS IDENTIFICATION MICROTUBULE-ASSOCIATED PROTEINS NEUROFILAMENTS PAIRED HELICAL FILAMENT PHOSPHATE ANALYSIS RECOGNIZES TAU-PROTEINhaPhosphate Analysis and Dephosphorylation of Modified Tau Associated with Paired Helical FilamentsBrain Research 597e2209-219h 4 Dec- 4136,%Ktistakis, N.T. Thomas, D. Roth, M.G. 1990AMINO-ACID SEQUENCE CDNA CLONES COATED PITS CYTOPLASMIC DOMAIN ENDOCYTOSIS FC-RECEPTOR INFLUENZA-VIRUS HEMAGGLUTININ LDL RECEPTOR MANNOSE 6-PHOSPHATE RECEPTOR MESSENGER-RNAtmCharacteristics of the Tyrosine Recognition Signal for Internalization of Transmembrane Surface Glycoproteins6Journal of Cell Biologyn 111i4 1393-1407 Octl 4135.'Ktistakis, N.T. Linder, M.E. Roth, M.G. 1992haCELLS ENDOPLASMIC-RETICULUM INTRACELLULAR-TRANSPORT MASTOPARAN RAT HEPATOCYTES SECRETORY PROTEINSZTAction of Brefeldin-A Blocked by Activation of a Pertussis-Toxin-Sensitive G-Protein Nature 356 6367344-346N 26 Mar,&Kubelka, J. Eaton, W.A. Hofrichter, J. 2003@:Experimental tests of villin subdomain folding simulations"Journal of Molecular Biology 329625-630o JAHM 4138& Kubo, T. Mizobata, T. Kawata, Y. 1993ATP HYDROLYSIS CHLORIDE-DENATURED RHODANESE COOPERATIVITY DETERGENT ESCHERICHIA-COLI MOLECULAR CHAPERONE PROTEIN PURIFICATION RIBULOSE BISPHOSPHATE CARBOXYLASE SURFACE|Refolding of Yeast Enolase in the Presence of the Chaperonin GroE - The Nucleotide Specificity of GroE and the Role of GroES&Journal of Biological Chemistry 268r26 19346-19351 15 Sep 4137B;Kubo, S. Chino, N. Watanaba, T.X. Kimura, T. Sakakibara, S.O 1993>7CONUS-GEOGRAPHUS MUSCLE SODIUM-CHANNELS PEPTIDES TOXINS^XSolution Synthesis of mu-Conotoxin GIIIB -Optimization of the Oxidative Folding ReactionPeptide Research62 66-72Mar-Apr 4139jcKubota, H. Willison, K. Ashworth, A. Nozaki, M. Miyamoto, H. Yamamoto, H. Matsushiro, A. Morita, T. 1992CHAPERONE CPG-RICH REGION DNA ELEMENT EUKARYOTIC TRANSCRIPTION EXON-INTRON GENOMIC DNA MESSENGER-RNA NUCLEOTIDE-SEQUENCE POLYMERASE PROMOTER PROTEIN REGULATORY ELEMENT RNA TRANSCRIPTION FACTOR TRANSCRIPTION START POINTXQStructure and Expression of the Gene Encoding Mouse t-Complex Polypeptide (Tcp-1) Gene 1202 207-215 21 Oct 4140NGKuby, S.A. Fleming, G. Alber, T. Richardson, D. Takenaka, H. Hamada, M. 1991Studies on yeast nucleoside triphosphate-nucleoside diphosphate transphosphorylase (nucleoside diphosphokinase). IV. Steady-state kinetic properties with thymidine nucleotides (including 3'-azido-3'-deoxythymidine analogues) Enzyme45 1-2X 1-13 4141*$Kudlicki, W. Kramer, G. Hardesty, B. 1992"IDENTIFICATION POLYPEPTIDES rkHigh Efficiency Cell-Free Synthesis of Proteins -Refinement of the Coupled Transcription/Translation SystemoAnalytical Biochemistrye 206w2389-393 Novu YNCtb1;'A1W'A4:'A8 'A8'A$UA$Ulpha1Ub1\01_01`020201_010121`21\2011U30121200 2i+ i+ d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d/d0U0 V0 030C000000000$0000 N0#0&C0&B0&A0&0]00t00 000!f0)0!01 1 s33z330!01!?122W3r1/54G45 -56r6!7/78G89*100]0.R.A.A.A.A.A.IA.A.A.A.A/A/A/AAAA&AwA AmA/AAAMAAlAsA/A/A/A/A/A/A/"A/%A&A/*A'SAA8A A)"AAA(A/>A/DA/EA/FA/HA/JA/KA/MA/NA/WA/]A/nA/vA/wA/hAh/Ah/Ah/AEMBRANE NASCENT PREPROLACTIN SACCHAROMYCES-CEREVISIAE SCHIZOSACCHAROMYCES-POMBE SECRETORY PROTEINBinding Sites of the 9-Kilodalton and 14-Kilodalton Heterodimeric Protein Subunit of the Signal Recognition Particle (SRP) Are Contained Exclusively in the Alu Domain of SRP-RNA and Contain a Sequence Motif That Is Conserved in Evolution$Molecular and Cellular Biology118 3949-3959 Augo 7571RKStruck, J.C.R. Far, R.K. Schroder, W. Hucho, F. Toschka, H.Y. Erdmann,.5 Molecular. E. E.F E* E. E. E. E. E. E. E. E. E. E. E. E. E. E E E. E. E. E. E. E. E. E/ E Ew E/" E/% E/& E  E/1 E( E/G E/N E/P E/Q E/T E/U E/[ E/g E/k E/l E/ E/ E/{ E- E-  E. E/B E/B E/B EB/ EB/ EB/ EB/ EB/ E.h Eh. E.h E(Whereasther ~ich/lll&l(Ll*l,l let-ktteII(ley 1 I,cknerdened!edmannlcoxZd*k_kinsonldliams Qsonnfieldl terhalterrskottth^o (o o Jo6oowooooooooo!oEo':oo ao izii6ii!i'Hi(i)i*i+i-i inoo-"o%out= tinghofer#:olfenden}ng{odson{rkt&uld rightu%underlichtthrichthrich WW19945*5,5.5-5<55555f5555*55 +5 D5 I5 h5 5 5 5 5!5!@5!G5!V5!i5" 5".5"95"C5"5"5(5"5# 5"5#5#5$5$R5$k5$5$5$5(5%c5%{5'W5'W5'W5'W5'W5'W5'W5'W5'W5'W5'W5'W5 Iwata1993$ Iwata1993" Iwata1993 Iyer1973v Iyer19933 Iyer1993 Izadyar1993 Izard1996' Izatt1976 Izotov1993 Izumi1992% Izumi1993! Izumihara1991 Izumiya1971% Izutsu19939)R J.19979Jaattela1992Jaattela1992+Jaattela1998$c Jablonsky1993+P Jabs19988 Jacb19699 Jacchieri1993c Jack19829 Jack1993v Jackson1977 Jack"NMR"o"o"o"o"o"o#o# o#o)o)o#Zo&o#co#mo#o*o#o#o#o#o#o*o#o#o#o$o*}o$o$0o$:o$Uo$Xo$[o$Zo$Yo$]o$\o*o$o$o%o% o%o%o%0o&o%Bo%Ko%Ro%To%ZoZ%oZ%oZ%o%Zo%Zo%Zo%Zo%Zo%Zo%Zo%Zo)+ BIochemistry ir i i+` ir i+a i i( i'P io i%  i+r i'R i'Q i i+} i+ i S i+ i+ i+ i+ i+ i+ i+ i+ i+ i+ i+ i* i#U i( i- i* i3 i+ i+ i+ i+ i, i, i i, i, i, i, i, i, i, i, i, i, i, i, i, i, i, i, i, i, i, i$ Molecular$ n$ n$" n$' n$/ n$4 n$5 n$6 n$K n$S n$` n$a n$ n$ n* n( n$ n$ n$ n$ n$ n$ n$ n$ n) n%/ n& n%< n%W n%^ n%f n%r n%s n% n% n) n% n% n% n% n% n% n% n% n% n% n% n% n& n& n& n& n& n( n&+ n&? n&G n&G n&G n&G n&G n&G n<6Mori, H. Araki, M. Hikita, C. Tagaya, M. Mizushima, S. 1997haThe Hydrophobic Region of Signal Peptides is Involved in the Interaction with Membrane-bound SecA$Biochimica et Biophysica Actay 1326 23-36,%Mori, S. van Zijl, P.C.M. Shortle, D. 1997Measurement of water-amide proton exchange rates in the denatured state of staphylococcal nuclease by a magnetization transfer technique.0*Proteins: Structure, Function and Genetics28325-332 SJE"2x8 5272,%Morelli, M.A.C. Pastore, A. Motta, A. 1992CALCITONIN CONFORMATIONAL FLEXIBILITY DISTANCE RESTRAINTS H 1 NMR MODEL MOLECULAR-DYNAMICS MOTION PEPTIDES PROGRAM PROTEIN REFINEMENT SDS SIMULATION TIME-AVERAGED DISTANCE NMR RESTRAINTSDynamic Properties of Salmon Calcitonin Bound to Sodium Dodecyl Sulfate Micelles - A Restrained Molecular Dynamics Study from NMR Data"Journal of Biomolecular NMR24335-348 Jul`>8Morello, J.P. Petaja-Repo, U.E. Bichet, D.G. Bouvier, M. 2000B;Pharmacological chaperones: a new twist on receptor folding("Trends in Pharmacological Sciences2112466-469 12/21 KSRd 5273LEMoreno, F. Fowler, A.V. Hall, M. Silhavy, T.J. Zabin, I. 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Burgoyne, R.D.` 1993ADP-RIBOSYLATION FACTOR BREFELDIN-A CALCIUM CATECHOLAMINE SECRETION CHROMAFFIN CELL DEPENDENT EXOCYTOSIS EXCHANGE EXOCYTOSIS FUSION GTP-BINDING PROTEIN GUANINE-NUCLEOTIDE RELEASE VESICLES VESICULAR TRANSPORTA Synthetic Peptide of the N-Terminus of ADP-Ribosylation Factor (ARF) Inhibits Regulated Exocytosis in Adrenal Chromaffin Cells FEBS Letters 329B 1-2121-124 23 AugMEMBRANEHolooooooo,o4o7o)o)ooo No Zo o!o!'o!o!o"2o"4o"xo"wo"yo# o#0o#o#o$&o$Qo$o$o%&o%'o%o%o%o&o&o)%o)1o))o+Xo+[o+\o+_o+do'Jo+go+ho+io+jo+lo&oo)Do+qo'Pooo)2o5retrieve5o5o5o6o6o6o6o6o6o6o6o6o6 o6 o6 o6 o6o6o6o6o6o6o6o6o6o6o6o6o6o6 o6!o6"o6#o6$o6%o6&o6'o6(o6)o6*o6+o6-o6.o6/o61o62o63o64o65o66o67o68o69o6:o6<o6=o6?o6@o6Ao6Bo6Bo6Bo6-And61a62a63a64a65a67a68a69a6:a6;a6<a6=a6>a6?a6@a6Aa6Ba6Ca6Da6Ea6Ga6Ha6Ia6Ja6Ka6La6Ma6Na6Oa6Pa6Qa6Ra6Sa6Ta6Ua6Wa6Xa6Ya6Za6[a6\a6]a6^a6_a6`a6aa6ba6ea6fa6ga6ha6ia6ja6ma6na6pa6ra6sa6ta6ua6va6va6va")thermodynamics"|l#Rl#ql$l%rl%sl%tl%l&l)6l+_l+ql'Pl'Ql&l#Lll/l/l/l/l/l/l/l/l/l/l/l/l/l/l/l/l/l/l/ll/l/l4l4tl%Dl5l5l6l6l6l6l6l6l6l6'l6(l6)l6-l68l6:l6Cl6Dl6Gl6Hl:  coOperativity  r V r _ r  r  r 6 r  r r r( r r< r r  r f r" r# r,K r,L r-l r/ r0 r0 r1 r2[ r3, r33 r4] r4i r# r4 r5 r  r r  r  r  r  r  r \ r  r r r r^ r r r r r r"+ r" r rC r6 r  r& r)( r6 r8 rCrdinate#q d+} d+ d6 d8 d dp i2 l8 l9L l#u l  l6 l8* l8@ l8F l8Y l8 l" lys7 s8 s s" i i1 i7 i7n i i id i"E i+ i6 i7 i7n i7p i8I i( ingC r6 r  r& r)( rCrdinate#q d+} d+ d dp i#u l  l" ly s i" i i id i"E i+ i( ingg311-319  JanhbMorelle, N. 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