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Volumn 310, Issue 1, 2001, Pages 27-32

Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long-range order to folding rate prediction

Author keywords

Contact order; Folding rate; Long range order; Protein folding; Structural classes

Indexed keywords

PROTEIN;

EID: 0035967862     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4775     Document Type: Article
Times cited : (293)

References (17)
  • 3
    • 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
  • 10
    • 0028868995 scopus 로고
    • The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
    • (1995) J. Mol. Biol. , vol.254 , pp. 260-288
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.