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Volumn 81, Issue 2, 2001, Pages 710-714

Heat capacity of protein folding

Author keywords

[No Author keywords available]

Indexed keywords

MYOGLOBIN;

EID: 0034909359     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(01)75735-9     Document Type: Article
Times cited : (12)

References (33)
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    • Amino acid conformational preferences and solvation of polar backbone atoms in peptides and proteins
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  • 3
    • 0035364761 scopus 로고    scopus 로고
    • Two-state protein model with water interactions: Influence of temperature on the intrinsic viscosity of myoglobin
    • in press
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  • 12
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  • 24
    • 0002693020 scopus 로고
    • Physical basis of the stability of the folded conformations of proteins
    • T. E. Creighton, editor. W. H. Freeman and Company, New York
    • (1992) Protein Folding
    • Privalov, P.L.1
  • 28
    • 0001775540 scopus 로고
    • Folded and unfolded proteins: An introduction
    • T. E. Creighton, editor. W. H. Freeman and Company, New York
    • (1992) Protein Folding
    • Richards, F.M.1
  • 29
    • 0022248941 scopus 로고
    • Calculations of electrostatic energies in proteins. The energetics of ionized groups in bovine pancreatic trypsin inhibitor
    • (1985) J. Mol. Biol. , vol.185 , pp. 389-404
    • Russell, S.T.1    Warshel, A.2
  • 30
    • 0028856228 scopus 로고
    • The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions by NMR and CD spectroscopy
    • (1995) Biochemistry , vol.34 , pp. 15895-15905
    • Wang, Y.1    Shortle, D.2
  • 31
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    • Theoretical studies of enzymic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.