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Volumn 118, Issue 29, 1996, Pages 6975-6985

Stereochemical requirements for β-hairpin formation: Model studies with four-residue peptides and depsipeptides

Author keywords

[No Author keywords available]

Indexed keywords

DEPSIPEPTIDE; DICHLOROMETHANE; GLOBULAR PROTEIN; GLYCOLIC ACID; LACTIC ACID; TETRAPEPTIDE;

EID: 0029931671     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja960429j     Document Type: Article
Times cited : (256)

References (55)
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    • Leading references on β-sheet protein design efforts: (a) Kullmann, W. J. Med. Chem. 1984, 27, 106. (b) Klauser, S.; Gantner, K.; Salgam, P.; Gutte, B. Biochem. Biophys. Res. Commun. 1991, 179, 1212. (c) Quinn, T. P.; Tweedy, N. B.; Williams, R. W.; Richardson, J. S.; Richardson, D. C. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 8747. (d) Van, Y.; Erickson, B. W. Protein Sci. 1994, 3, 1069.
    • (1984) J. Med. Chem. , vol.27 , pp. 106
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  • 20
    • 0026045860 scopus 로고
    • Leading references on β-sheet protein design efforts: (a) Kullmann, W. J. Med. Chem. 1984, 27, 106. (b) Klauser, S.; Gantner, K.; Salgam, P.; Gutte, B. Biochem. Biophys. Res. Commun. 1991, 179, 1212. (c) Quinn, T. P.; Tweedy, N. B.; Williams, R. W.; Richardson, J. S.; Richardson, D. C. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 8747. (d) Van, Y.; Erickson, B. W. Protein Sci. 1994, 3, 1069.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1212
    • Klauser, S.1    Gantner, K.2    Salgam, P.3    Gutte, B.4
  • 21
    • 0028587717 scopus 로고
    • Leading references on β-sheet protein design efforts: (a) Kullmann, W. J. Med. Chem. 1984, 27, 106. (b) Klauser, S.; Gantner, K.; Salgam, P.; Gutte, B. Biochem. Biophys. Res. Commun. 1991, 179, 1212. (c) Quinn, T. P.; Tweedy, N. B.; Williams, R. W.; Richardson, J. S.; Richardson, D. C. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 8747. (d) Van, Y.; Erickson, B. W. Protein Sci. 1994, 3, 1069.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 8747
    • Quinn, T.P.1    Tweedy, N.B.2    Williams, R.W.3    Richardson, J.S.4    Richardson, D.C.5
  • 22
    • 0028309466 scopus 로고
    • Leading references on β-sheet protein design efforts: (a) Kullmann, W. J. Med. Chem. 1984, 27, 106. (b) Klauser, S.; Gantner, K.; Salgam, P.; Gutte, B. Biochem. Biophys. Res. Commun. 1991, 179, 1212. (c) Quinn, T. P.; Tweedy, N. B.; Williams, R. W.; Richardson, J. S.; Richardson, D. C. Proc. Natl. Acad. Sci. U.S.A. 1994, 91, 8747. (d) Van, Y.; Erickson, B. W. Protein Sci. 1994, 3, 1069.
    • (1994) Protein Sci. , vol.3 , pp. 1069
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  • 26
    • 0347765149 scopus 로고
    • Short peptides folded into β-hairpins under non-aqueous conditions: (a) Ueki, T.; Bando, S.; Ashida, T.; Kakudo, M. Acta Crystallogr. 1971, B27, 2219. (b) Karle, I. L.; Kishore, R.; Raghothama, S.; Balaram, P. J. Am. Chem. Soc. 1988, 110, 1958. (c) Awasthi, S. K.; Raghothama, S.; Balaram, P. Biochem. Biophys. Res. Commun. 1995, 216, 375.
    • (1971) Acta Crystallogr. , vol.B27 , pp. 2219
    • Ueki, T.1    Bando, S.2    Ashida, T.3    Kakudo, M.4
  • 27
    • 0023835296 scopus 로고
    • Short peptides folded into β-hairpins under non-aqueous conditions: (a) Ueki, T.; Bando, S.; Ashida, T.; Kakudo, M. Acta Crystallogr. 1971, B27, 2219. (b) Karle, I. L.; Kishore, R.; Raghothama, S.; Balaram, P. J. Am. Chem. Soc. 1988, 110, 1958. (c) Awasthi, S. K.; Raghothama, S.; Balaram, P. Biochem. Biophys. Res. Commun. 1995, 216, 375.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1958
    • Karle, I.L.1    Kishore, R.2    Raghothama, S.3    Balaram, P.4
  • 28
    • 0028972051 scopus 로고
    • Short peptides folded into β-hairpins under non-aqueous conditions: (a) Ueki, T.; Bando, S.; Ashida, T.; Kakudo, M. Acta Crystallogr. 1971, B27, 2219. (b) Karle, I. L.; Kishore, R.; Raghothama, S.; Balaram, P. J. Am. Chem. Soc. 1988, 110, 1958. (c) Awasthi, S. K.; Raghothama, S.; Balaram, P. Biochem. Biophys. Res. Commun. 1995, 216, 375.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 375
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  • 43
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    • note
    • A recently described β-sheet protein design (ref 4d) includes the use of D-residues at positions intended to form two-residue β-hairpin loops.
  • 44
    • 0028843733 scopus 로고
    • DL, indicates that side chains, with the correct configuration, are required on the terminal residues for complete β-hairpin formation. These terminal residue side chains presumably decrease the number of non-hairpin conformations available to the backbone, thus decreasing the loss of conformational entropy associated with adoption of the hairpin folding pattern.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10411
    • Gardner, R.R.1    Gellman, S.H.2
  • 45
    • 0028865129 scopus 로고
    • Searle, M. S.; Williams, D. H.; Rackman, L. C. Nature Struct. Biol. 1995, 2, 999. For β-hairpin folding, in water, of a 16-residue peptide that lacks proline, see: Blanco, F. J.; Rivas, G.; Serrano, L. Nature Struct. Biol. 1994, 1, 584.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 999
    • Searle, M.S.1    Williams, D.H.2    Rackman, L.C.3
  • 46
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    • Searle, M. S.; Williams, D. H.; Rackman, L. C. Nature Struct. Biol. 1995, 2, 999. For β-hairpin folding, in water, of a 16-residue peptide that lacks proline, see: Blanco, F. J.; Rivas, G.; Serrano, L. Nature Struct. Biol. 1994, 1, 584.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 584
    • Blanco, F.J.1    Rivas, G.2    Serrano, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.