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Volumn 313, Issue 1, 2001, Pages 171-180

Roles of native topology and chain-length scaling in protein folding: A simulation study with a ḡ-like model

Author keywords

Contact order; Denatured state; Folding rate; Transition state; value

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MYOGLOBIN; PROTEIN A;

EID: 0035850732     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5037     Document Type: Article
Times cited : (333)

References (34)
  • 4
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 6
    • 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.A.1    Otzen, D.E.2    Fersht, A.R.3
  • 26
    • 0034685604 scopus 로고    scopus 로고
    • Topological and energetic factors: What determines the structural details of the transition state ensemble and "en-route" intermediates for protein folding?
    • (2000) J. Mol. Biol. , vol.298 , pp. 937-953
    • Clementi, C.1    Nymeyer, H.2    Onuchic, J.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.