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Volumn 309, Issue 5, 2001, Pages 1177-1187

Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c551 from Pseudomonas aeruginosa

Author keywords

Chevron plot; Folding kinetics; Stability; Transition states; values

Indexed keywords

CYTOCHROME C; GLUTAMINE; HEME; HISTIDINE; IRON; LYSINE; METHIONINE; PROLINE; PROPIONIC ACID;

EID: 0035933343     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4728     Document Type: Article
Times cited : (33)

References (44)
  • 6
    • 0000384736 scopus 로고    scopus 로고
    • Alternative explanations for "multistate" kinetics in protein folding: Transient aggregation and changing transition-state ensembles
    • (1998) Accts Chem. Res. , vol.31 , pp. 765-772
    • Oliveberg, M.1
  • 7
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 18
    • 0032496419 scopus 로고    scopus 로고
    • Protein folding and protein evolution: Common folding nucleus in different subfamilies of c-type cytochromes?
    • (1998) J. Mol. Biol. , vol.278 , pp. 655-666
    • Ptitsyn, O.B.1
  • 21
    • 0022399830 scopus 로고
    • Helix movements and the reconstruction of the haem pocket during the evolution of the cytochrome c family
    • (1985) J. Mol. Biol. , vol.182 , pp. 151-158
    • Chothia, C.1    Lesk, A.M.2
  • 26
    • 0028569153 scopus 로고
    • Protein denaturation with guanidine hydrocloride or urea provides a different estimate of stability depending on the contribution of electrostatic interactions
    • (1994) Protein Sci. , vol.3 , pp. 1984-1991
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 28
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 32
    • 0027163998 scopus 로고
    • Protein folding and stability: The pathway of folding of barnase
    • (1993) FEBS Letters , vol.325 , pp. 5-16
    • Fersht, A.R.1
  • 41
    • 0029943662 scopus 로고    scopus 로고
    • New approach to the study of transient protein conformations: The formation of a semiburied salt link in the folding pathway of barnase
    • (1996) Biochemistry , vol.35 , pp. 6795-6805
    • Oliveberg, M.1    Fersht, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.