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Volumn 306, Issue 4, 2001, Pages 837-850

Native topology or specific interactions: What is more important for protein folding?

Author keywords

Free energy surface; Implicit solvation model; Molecular dynamics simulation; Structured peptide folding; Three stranded antiparallel sheet

Indexed keywords

GLYCINE; PEPTIDE; SERINE;

EID: 0035793713     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4400     Document Type: Article
Times cited : (57)

References (47)
  • 2
    • 0034604105 scopus 로고    scopus 로고
    • A surprising simplicity to protein folding
    • (2000) Nature , vol.405 , pp. 39-42
    • Baker, D.1
  • 19
    • 0032561237 scopus 로고    scopus 로고
    • Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
    • (1998) Science , vol.282 , pp. 740-744
    • Duan, Y.1    Kollman, P.A.2
  • 36
    • 0345062357 scopus 로고    scopus 로고
    • Universally conserved positions in protein folds: Reading evolutionary signals about stability, folding kinetics and function
    • (1999) J. Mol. Biol. , vol.291 , pp. 177-196
    • Mirny, L.A.1    Shakhnovich, E.I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.