메뉴 건너뛰기




Volumn 12, Issue 8, 2004, Pages 1507-1518

10 Residue folded peptide designed by segment statistics

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID DERIVATIVE; CHIGNOLIN; PEPTIDE; UNCLASSIFIED DRUG; WATER;

EID: 4143145167     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2004.05.022     Document Type: Article
Times cited : (272)

References (47)
  • 1
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen C.B., Scheraga H.A. Experimental and theoretical aspects of protein folding. Adv. Protein Chem. 29:1975;205-300
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 2
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y., Milne J.S., Mayne L., Englander S.W. Primary structure effects on peptide group hydrogen exchange. Proteins. 17:1993;75-86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 3
    • 0001603062 scopus 로고
    • Submarine hydrothermal vents and associated gradient environments as sites for the origin and evolution of life
    • Baross J.A., Hoffman S.E. Submarine hydrothermal vents and associated gradient environments as sites for the origin and evolution of life. Orig. Life Evol. Biosph. 15:1985;327-345
    • (1985) Orig. Life Evol. Biosph. , vol.15 , pp. 327-345
    • Baross, J.A.1    Hoffman, S.E.2
  • 4
    • 0028500779 scopus 로고
    • A short linear peptide that folds into a native stable beta-hairpin in aqueous solution
    • Blanco F.J., Rivas G., Serrano L. A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nat. Struct. Biol. 1:1994;584-590
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 584-590
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3
  • 6
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH
    • Bundi A., Wüthrich K. 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-L-Ala-OH. Biopolymers. 18:1979;285-297
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 8
    • 0035826776 scopus 로고    scopus 로고
    • Tryptophan zippers: Stable, monomeric beta-hairpins
    • Erratum: Proc. Natl. Acad. Sci. USA 99, 9081.
    • Cochran A.G., Skelton N.J., Starovasnik M.A. Tryptophan zippers. stable, monomeric beta-hairpins Proc. Natl. Acad. Sci. USA. 98:2001;5578-5583. Erratum: Proc. Natl. Acad. Sci. USA 99, 9081.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5578-5583
    • Cochran, A.G.1    Skelton, N.J.2    Starovasnik, M.A.3
  • 9
  • 10
    • 0028335799 scopus 로고
    • Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue
    • de Prat Gay G., Fersht A.R. Generation of a family of protein fragments for structure-folding studies. 1. Folding complementation of two fragments of chymotrypsin inhibitor-2 formed by cleavage at its unique methionine residue. Biochemistry. 33:1994;7957-7963
    • (1994) Biochemistry , vol.33 , pp. 7957-7963
    • De Prat Gay, G.1    Fersht, A.R.2
  • 14
    • 0032246263 scopus 로고    scopus 로고
    • Minimal model systems for beta sheet secondary structure in proteins
    • Gellman S.H. Minimal model systems for beta sheet secondary structure in proteins. Curr. Opin. Chem. Biol. 2:1998;717-725
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 717-725
    • Gellman, S.H.1
  • 15
    • 0021801342 scopus 로고
    • Genes-in-pieces revisited
    • Gilbert W. Genes-in-pieces revisited. Science. 228:1985;823-824
    • (1985) Science , vol.228 , pp. 823-824
    • Gilbert, W.1
  • 16
    • 0028716614 scopus 로고
    • Contributions of tryptophan side chains to the circular dichroism of globular proteins: Exciton couplets and coupled oscillators
    • Grishina I.B., Woody R.W. Contributions of tryptophan side chains to the circular dichroism of globular proteins. exciton couplets and coupled oscillators Faraday Discuss. 99:1994;245-262
    • (1994) Faraday Discuss. , vol.99 , pp. 245-262
    • Grishina, I.B.1    Woody, R.W.2
  • 17
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz Y., Gerstein M., Chothia C. Volume changes on protein folding. Structure. 2:1994;641-649
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 18
    • 0026633609 scopus 로고
    • Singular value decomposition: Application to analysis of experimental data
    • Henry E.R., Hofrichter J. Singular value decomposition. application to analysis of experimental data Methods Enzymol. 210:1992;129-192
    • (1992) Methods Enzymol. , vol.210 , pp. 129-192
    • Henry, E.R.1    Hofrichter, J.2
  • 19
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm U., Sander C. Enlarged representative set of protein structures. Protein Sci. 3:1994;522-524
    • (1994) Protein Sci. , vol.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 20
    • 0033604829 scopus 로고    scopus 로고
    • Fragment reconstitution of a small protein: Folding energetics of the reconstituted immunoglobulin binding domain B1 of streptococcal protein G
    • Honda S., Kobayashi N., Munekata E., Uedaira H. Fragment reconstitution of a small protein. folding energetics of the reconstituted immunoglobulin binding domain B1 of streptococcal protein G Biochemistry. 38:1999;1203-1213
    • (1999) Biochemistry , vol.38 , pp. 1203-1213
    • Honda, S.1    Kobayashi, N.2    Munekata, E.3    Uedaira, H.4
  • 21
    • 0034645735 scopus 로고    scopus 로고
    • Thermodynamics of a beta-hairpin structure: Evidence for cooperative formation of folding nucleus
    • Honda S., Kobayashi N., Munekata E. Thermodynamics of a beta-hairpin structure. evidence for cooperative formation of folding nucleus J. Mol. Biol. 295:2000;269-278
    • (2000) J. Mol. Biol. , vol.295 , pp. 269-278
    • Honda, S.1    Kobayashi, N.2    Munekata, E.3
  • 22
    • 0033042555 scopus 로고    scopus 로고
    • Stability and folding of domain proteins
    • Jaenicke R. Stability and folding of domain proteins. Prog. Biophys. Mol. Biol. 71:1999;155-241
    • (1999) Prog. Biophys. Mol. Biol. , vol.71 , pp. 155-241
    • Jaenicke, R.1
  • 23
    • 0026703842 scopus 로고
    • Analysis of circular dichroism spectra
    • Johnson W.C. Analysis of circular dichroism spectra. Methods Enzymol. 210:1992;426-447
    • (1992) Methods Enzymol. , vol.210 , pp. 426-447
    • Johnson, W.C.1
  • 24
    • 0017251893 scopus 로고
    • Protein-folding dynamics
    • Karplus M., Weaver D.L. Protein-folding dynamics. Nature. 260:1976;404-406
    • (1976) Nature , vol.260 , pp. 404-406
    • Karplus, M.1    Weaver, D.L.2
  • 26
    • 0029055171 scopus 로고
    • Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution
    • Kobayashi N., Honda S., Yoshii H., Uedaira H., Munekata E. Complement assembly of two fragments of the streptococcal protein G B1 domain in aqueous solution. FEBS Lett. 366:1995;99-103
    • (1995) FEBS Lett. , vol.366 , pp. 99-103
    • Kobayashi, N.1    Honda, S.2    Yoshii, H.3    Uedaira, H.4    Munekata, E.5
  • 27
    • 0034733005 scopus 로고    scopus 로고
    • Role of side-chains in the cooperative beta-Hairpin folding of the short c-terminal fragment derived from streptococcal protein G
    • Kobayashi N., Honda S., Yoshii H., Munekata E. Role of side-chains in the cooperative beta-Hairpin folding of the short c-terminal fragment derived from streptococcal protein G. Biochemistry. 39:2000;6564-6571
    • (2000) Biochemistry , vol.39 , pp. 6564-6571
    • Kobayashi, N.1    Honda, S.2    Yoshii, H.3    Munekata, E.4
  • 29
  • 31
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of beta-hairpin formation in protein G folding
    • McCallister E.L., Alm E., Baker D. Critical role of beta-hairpin formation in protein G folding. Nat. Struct. Biol. 7:2000;669-673
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 33
    • 0038502170 scopus 로고    scopus 로고
    • Folding dynamics and mechanism of beta-hairpin formation
    • Muñoz V., Thompson P.A., Hofrichter J., Eaton W.A. Folding dynamics and mechanism of beta-hairpin formation. Nature. 390:1997;196-199
    • (1997) Nature , vol.390 , pp. 196-199
    • Muñoz, V.1    Thompson, P.A.2    Hofrichter, J.3    Eaton, W.A.4
  • 35
    • 0033529908 scopus 로고    scopus 로고
    • Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G
    • Pande V.S., Rokhsar D.S. Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G. Proc. Natl. Acad. Sci. USA. 96:1999;9062-9067
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 9062-9067
    • Pande, V.S.1    Rokhsar, D.S.2
  • 36
    • 0032040411 scopus 로고    scopus 로고
    • Protein folding: Nucleation and compact intermediates
    • Ptitsyn O.B. Protein folding. nucleation and compact intermediates Biochemistry (Mosc.). 63:1998;367-373
    • (1998) Biochemistry (Mosc.) , vol.63 , pp. 367-373
    • Ptitsyn, O.B.1
  • 37
    • 0034743055 scopus 로고    scopus 로고
    • Peptide models of protein beta-sheets: Design, folding and insights into stabilising weak interactions
    • Searle M.S. Peptide models of protein beta-sheets. design, folding and insights into stabilising weak interactions J. Chem. Soc. Perkin Trans. I. 2:2001;1011-1020
    • (2001) J. Chem. Soc. Perkin Trans. I , vol.2 , pp. 1011-1020
    • Searle, M.S.1
  • 39
    • 0034581611 scopus 로고    scopus 로고
    • The relationship between sequence and structure in elementary folding units
    • Serrano L. The relationship between sequence and structure in elementary folding units. Adv. Protein Chem. 53:2000;49-85
    • (2000) Adv. Protein Chem. , vol.53 , pp. 49-85
    • Serrano, L.1
  • 40
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich E., Abkevich V., Ptitsyn O. Conserved residues and the mechanism of protein folding. Nature. 379:1996;96-98
    • (1996) Nature , vol.379 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 41
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle D., Ackerman M.S. Persistence of native-like topology in a denatured protein in 8 M urea. Science. 293:2001;487-489
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 42
    • 0026351935 scopus 로고
    • Conformation of beta hairpins in protein structures: Classification and diversity in homologous structures
    • Sibanda B.L., Thornton J.M. Conformation of beta hairpins in protein structures. classification and diversity in homologous structures Methods Enzymol. 202:1991;59-82
    • (1991) Methods Enzymol. , vol.202 , pp. 59-82
    • Sibanda, B.L.1    Thornton, J.M.2
  • 43
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons K.T., Kooperberg C., Huang E., Baker D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268:1997;209-225
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 44
    • 0023645325 scopus 로고
    • Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN
    • Wagner G., Braun W., Havel T.F., Schaumann T., Go N., Wüthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196:1987;611-639
    • (1987) J. Mol. Biol. , vol.196 , pp. 611-639
    • Wagner, G.1    Braun, W.2    Havel, T.F.3    Schaumann, T.4    Go, N.5    Wüthrich, K.6
  • 45
    • 0043180474 scopus 로고    scopus 로고
    • Pisces: A protein sequence culling server
    • Wang G., Dunbrack R.L. Jr. Pisces. a protein sequence culling server Bioinformatics. 19:2003;1589-1591
    • (2003) Bioinformatics , vol.19 , pp. 1589-1591
    • Wang, G.1    Dunbrack Jr., R.L.2
  • 46
    • 0015597839 scopus 로고
    • Nucleation, rapid folding, and globular intrachain regions in proteins
    • Wetlaufer D.B. Nucleation, rapid folding, and globular intrachain regions in proteins. Proc. Natl. Acad. Sci. USA. 70:1973;697-701
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 697-701
    • Wetlaufer, D.B.1
  • 47
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart D.S., Sykes B.D., Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222:1991;311-333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.