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Volumn 311, Issue 5, 2001, Pages 1091-1104

Denatured state thermodynamics: Residual structure, chain stiffness and scaling factors

Author keywords

Cytochrome c; Denatured state; Guanidine hydrochloride; Protein folding; Random coil

Indexed keywords

CYTOCHROME C; GUANIDINE; HEME; HISTIDINE; MONOMER;

EID: 0035979801     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4909     Document Type: Article
Times cited : (60)

References (80)
  • 6
    • 0030032461 scopus 로고    scopus 로고
    • The denatured state (the other half of the folding equation) and its role in protein stability
    • (1996) FASEB J , vol.10 , pp. 27-34
    • Shortle, D.1
  • 13
    • 0027138868 scopus 로고
    • Partitioning the effects of changes in a protein to the folded or unfolded forms by using a thermodynamic cycle: A change in Escherichia coli thioredoxin does not affect the unfolded state
    • (1993) Biochemistry , vol.32 , pp. 12922-12927
    • Wynn, R.1    Richards, F.M.2
  • 15
    • 0030468993 scopus 로고    scopus 로고
    • Rapid formation of the native 14-38 disulfide bond in the early stages of BPTI folding
    • (1996) Biochemistry , vol.35 , pp. 16153-16164
    • Dadlez, M.1    Kim, P.S.2
  • 17
    • 0031584267 scopus 로고    scopus 로고
    • A histidine variant of yeast iso-1-cytochrome c that strongly affects the energetics of the denatured state
    • (1997) J. Mol. Biol , vol.268 , pp. 816-821
    • Godbole, S.1    Bowler, B.E.2
  • 23
    • 0033523097 scopus 로고    scopus 로고
    • Reinterpretation of GCN4-N1 folding kinetics: Partial helix formation precedes dimerization in coiled coil folding
    • (1999) J. Mol. Biol. , vol.289 , pp. 205-209
    • Myers, J.K.1    Oas, T.G.2
  • 30
    • 0000114379 scopus 로고    scopus 로고
    • Time scales for the formation of the most probable tertiary contact in proteins with application to cytochrome c
    • (1999) J. Phys. Chem. ser. B , vol.103 , pp. 608-610
    • Thirumulai, D.1
  • 32
    • 0032488914 scopus 로고    scopus 로고
    • Cytochrome c folding traps are not due solely to histidine-heme ligation: Direct demonstration of a role for N-terminal amino group-heme ligation
    • (1998) J. Mol. Biol , vol.275 , pp. 719-724
    • Hammack, B.1    Godbole, S.2    Bowler, B.E.3
  • 40
    • 0030022713 scopus 로고    scopus 로고
    • Thermodynamics of denaturation of staphylococcal nuclease mutants: An intermediate state in protein folding
    • (1996) FASEB J , vol.10 , pp. 67-74
    • Carra, J.H.1    Privalov, P.L.2
  • 42
    • 0033524433 scopus 로고    scopus 로고
    • Effect of pH on formation of a nativelike intermediate on the unfolding pathway of a Lys73 → His variant of yeast iso-1-cytochrome c
    • (1999) Biochemistry , vol.38 , pp. 487-495
    • Godbole, S.1    Bowler, B.E.2
  • 51
  • 52
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • (1993) Protein Sci , vol.2 , pp. 1551-1558
    • Betz, S.F.1
  • 60
    • 0030623398 scopus 로고    scopus 로고
    • An inverse correlation between loop length and stability in a four helix bundle
    • (1997) Fold. Des , vol.2 , pp. 67-75
    • Nagi, A.D.1    Regan, L.2
  • 61
    • 0027255302 scopus 로고
    • Dissecting the disulphide-coupled folding pathway of bovine pancreatic trypsin inhibitor: Forming the first disulphide bonds in analogues of the reduced protein
    • (1993) J. Mol. Biol , vol.232 , pp. 873-896
    • Darby, N.J.1    Crieghton, T.J.2
  • 68
    • 0023009068 scopus 로고
    • Inhibition of restriction endonuclease NciI cleavage by phosphorothioate groups and its application to oligonucleotide-directed mutagenesis
    • (1986) Nucl. Acids Res , vol.14 , pp. 9679-9698
    • Nakamaye, K.1    Eckstein, F.2
  • 77
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol , vol.113 , pp. 266-280
    • Pace, C.N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.