메뉴 건너뛰기




Volumn 124, Issue 6, 1998, Pages 1117-1123

Crystal structure analysis of collagen model peptide (Pro-Pro-Gly)10

Author keywords

Collagen; Hydration; Hydroxyproline; Model peptide; Triple helix

Indexed keywords

COLLAGEN; HYDROXYPROLINE; PEPTIDE;

EID: 0032445030     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022229     Document Type: Article
Times cited : (57)

References (27)
  • 1
    • 0029006974 scopus 로고
    • Collagens: Molecular biology, diseases and potential for therapy
    • Prockop, D.J. and Kivirikko, K.I. (1995) Collagens: molecular biology, diseases and potential for therapy. Annu. Rev. Biochem. 64, 403-434
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 403-434
    • Prockop, D.J.1    Kivirikko, K.I.2
  • 2
    • 0029645406 scopus 로고
    • Hydration structure of a collagen peptide
    • Bella, J., Brodsky, B., and Berman, H.M. (1995) Hydration structure of a collagen peptide. Structure 3, 893-906
    • (1995) Structure , vol.3 , pp. 893-906
    • Bella, J.1    Brodsky, B.2    Berman, H.M.3
  • 5
    • 0000523565 scopus 로고
    • Structure of collagen
    • Ramachandran, G.N. and Kartha, G. (1955) Structure of collagen. Nature 176, 593-595
    • (1955) Nature , vol.176 , pp. 593-595
    • Ramachandran, G.N.1    Kartha, G.2
  • 6
    • 32844463093 scopus 로고
    • The Structure of collagen
    • Rich, A. and Crick, F.H.C. (1955) The Structure of collagen. Nature 176, 915-916
    • (1955) Nature , vol.176 , pp. 915-916
    • Rich, A.1    Crick, F.H.C.2
  • 7
    • 32444451050 scopus 로고
    • The molecular structure of collagen
    • Rich, A. and Crick, F.H.C. (1961) The molecular structure of collagen. J. Mol. Biol. 3, 483-506
    • (1961) J. Mol. Biol. , vol.3 , pp. 483-506
    • Rich, A.1    Crick, F.H.C.2
  • 8
    • 0018400235 scopus 로고
    • Chain conformation in the collagen molecule
    • Fraser, R.D.B., MacRae, T.P., and Suzuki, E. (1979) Chain conformation in the collagen molecule. J. Mol. Biol. 129, 463-481
    • (1979) J. Mol. Biol. , vol.129 , pp. 463-481
    • Fraser, R.D.B.1    MacRae, T.P.2    Suzuki, E.3
  • 11
    • 84913411980 scopus 로고
    • LALS: A linked-atom least-squares reciprocal-space refinement system incorporating stereochemical restraints to supplement sparse diffraction data
    • Smith, P.J.C. and Arnott, S. (1978) LALS: A linked-atom least-squares reciprocal-space refinement system incorporating stereochemical restraints to supplement sparse diffraction data. Acta Cryst. A34, 3-11
    • (1978) Acta Cryst. , vol.A34 , pp. 3-11
    • Smith, P.J.C.1    Arnott, S.2
  • 14
    • 0027996196 scopus 로고
    • Crystal and molecular structure of a collagen-like peptide at 1.9 a resolution
    • Bella, J., Eaton, M., Brodsky, B., and Berman, H.M. (1994) Crystal and molecular structure of a collagen-like peptide at 1.9 A resolution. Science 266, 75-81
    • (1994) Science , vol.266 , pp. 75-81
    • Bella, J.1    Eaton, M.2    Brodsky, B.3    Berman, H.M.4
  • 17
    • 0001765479 scopus 로고
    • Structure of collagen at the molecular level
    • (Ramachandran, G.N., ed.) Academic Press, London
    • Ramachandran, G.N. (1967) Structure of collagen at the molecular level in Treatise of Collagen (Ramachandran, G.N., ed.) Vol. 1, pp. 103-183, Academic Press, London
    • (1967) Treatise of Collagen , vol.1 , pp. 103-183
    • Ramachandran, G.N.1
  • 18
    • 0037877123 scopus 로고
    • A system for X-ray crystallography and NMR
    • Yale University Press, New Haven and London
    • Brunger, A.T. (1992) A system for X-ray crystallography and NMR, X-PLOR Version 3.1, Yale University Press, New Haven and London
    • (1992) X-PLOR Version 3.1
    • Brunger, A.T.1
  • 19
    • 0030880598 scopus 로고    scopus 로고
    • SHELXL: High resolution refinement
    • Sweet, R.M. and Cater Jr, C.W., eds. Academic Press, Orlando, FL
    • Sheldrick, G.M. and Schneider, T.R. (1997) SHELXL: High resolution refinement in Methods in Enzymology (Sweet, R.M. and Cater Jr, C.W., eds.) Vol. 277, pp. 319-343, Academic Press, Orlando, FL
    • (1997) Methods in Enzymology , vol.277 , pp. 319-343
    • Sheldrick, G.M.1    Schneider, T.R.2
  • 22
    • 0028978764 scopus 로고
    • The occurrence of C-H⋯O hydrogen bond in proteins
    • Derewenda, Z.S., Lee, L., and Derewenda, V. (1995) The occurrence of C-H⋯O hydrogen bond in proteins. J. Mol. Biol. 252, 248-262
    • (1995) J. Mol. Biol. , vol.252 , pp. 248-262
    • Derewenda, Z.S.1    Lee, L.2    Derewenda, V.3
  • 24
    • 0030582683 scopus 로고    scopus 로고
    • α-H⋯O=C hydrogen bonds in a collagen triple helix
    • α-H⋯O=C hydrogen bonds in a collagen triple helix. J. Mol. Biol. 264, 732-742
    • (1996) J. Mol. Biol. , vol.264 , pp. 732-742
    • Bella, J.1    Berman, H.M.2
  • 25
    • 0026908646 scopus 로고
    • Thermodynamic substantiation of water-bridged collagen structure
    • Burjanadze, T.V. (1992) Thermodynamic substantiation of water-bridged collagen structure. Biopolymers 32, 941-949
    • (1992) Biopolymers , vol.32 , pp. 941-949
    • Burjanadze, T.V.1
  • 26
    • 0015852842 scopus 로고
    • A hypothesis on the role of hydroxyproline in stabilizing collagen structure
    • Ramachandran, G.N., Bansal, M., and Bhatnagar, R.S. (1973) A hypothesis on the role of hydroxyproline in stabilizing collagen structure. Biochim. Biophys. Acta 322, 166-171
    • (1973) Biochim. Biophys. Acta , vol.322 , pp. 166-171
    • Ramachandran, G.N.1    Bansal, M.2    Bhatnagar, R.S.3
  • 27
    • 0002145393 scopus 로고
    • Role of hydroxyproline in the stabilization of the collagen molecule via water molecules
    • Suzuki, E., Fraser, R.D.B., and MacRae, T.P. (1980) Role of hydroxyproline in the stabilization of the collagen molecule via water molecules. Int. J. Biol. Macromol. 2, 54-56
    • (1980) Int. J. Biol. Macromol. , vol.2 , pp. 54-56
    • Suzuki, E.1    Fraser, R.D.B.2    MacRae, T.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.