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Volumn 17, Issue 8-9, 1998, Pages 679-680

Does bound water contribute to the stability of collagen [1]

Author keywords

[No Author keywords available]

Indexed keywords

COLLAGEN; WATER;

EID: 0032415517     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90119-6     Document Type: Letter
Times cited : (34)

References (13)
  • 1
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • J. Bella B. Brodsky H.M. Berman Hydration structure of a collagen peptide Structure 3 1995 893 906
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 2
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution
    • J. Bella M. Eaton B. Brodsky H.M. Berman Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution Science 266 1994 75 81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 4
    • 0030865343 scopus 로고    scopus 로고
    • Versatile collagens in invertebrates
    • J. Engel Versatile collagens in invertebrates Science 277 1997 1785 1786
    • (1997) Science , vol.277 , pp. 1785-1786
    • Engel, J.1
  • 7
    • 0030590236 scopus 로고    scopus 로고
    • Glycosylated threonine but not 4-hydrxyproline dominates the triple helix stabilizing positions in the sequence of a hydrothermal vent worm cuticle collagen
    • K. Mann D.E. Mechling H.P. Bächinger C. Eckerskorn F. Gaill R. Timpl Glycosylated threonine but not 4-hydrxyproline dominates the triple helix stabilizing positions in the sequence of a hydrothermal vent worm cuticle collagen J. Mol. Biol. 261 1996 255 266
    • (1996) J. Mol. Biol. , vol.261 , pp. 255-266
    • Mann, K.1    Mechling, D.E.2    Bächinger, H.P.3    Eckerskorn, C.4    Gaill, F.5    Timpl, R.6
  • 9
    • 0020348367 scopus 로고
    • Stability of proteins
    • P.L. Privalov Stability of proteins Proteins which do not present a single cooperative system Adv. Protein Chem. 35 1982 1 104
    • (1982) , pp. 1-104
    • Privalov, P.L.1
  • 10
    • 0029006974 scopus 로고
    • Collagen: molecular biology, diseases and potentials for therapy
    • D.J. Prockop K.I. Kivirikko Collagen: molecular biology, diseases and potentials for therapy Ann. Rev. Biochem. 64 1995 403 434
    • (1995) Ann. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 11
    • 0023061930 scopus 로고
    • Structure and dynamics of water surrounding biomolecules
    • W. Saenger Structure and dynamics of water surrounding biomolecules Ann. Rev. Biophys. Chem. 16 1987 93 114
    • (1987) Ann. Rev. Biophys. Chem. , vol.16 , pp. 93-114
    • Saenger, W.1
  • 13
    • 0030670567 scopus 로고    scopus 로고
    • Gly-Pro-Arg confers stability similar to Gly-Pro-Hyp in the collagen triple-helix of host-guest peptides
    • W. Yang V.C. Chan A. Kirkpatrick J.A.M. Ramshaw B. Brodsky Gly-Pro-Arg confers stability similar to Gly-Pro-Hyp in the collagen triple-helix of host-guest peptides J. Biol. Chem. 272 1997 28837 28840
    • (1997) J. Biol. Chem. , vol.272 , pp. 28837-28840
    • Yang, W.1    Chan, V.C.2    Kirkpatrick, A.3    Ramshaw, J.A.M.4    Brodsky, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.