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Volumn 100, Issue 34, 1996, Pages 14540-14548

Optimizing potential functions for protein folding

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0000829596     PISSN: 00223654     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp960856j     Document Type: Article
Times cited : (44)

References (49)
  • 27
    • 38349181235 scopus 로고    scopus 로고
    • Bohr, H. Brunak, S. Eds.; CRC Press, Inc.: New York
    • Wolynes, P. G. In Protein Folds; Bohr, H. Brunak, S. Eds.; CRC Press, Inc.: New York, 1996; p 3, and references therein.
    • (1996) Protein Folds , pp. 3
    • Wolynes, P.G.1
  • 29
    • 85033069769 scopus 로고
    • Proceedings of the 1995 ACM/IEE Supercomputing Conference, December 3-8, 1995, San Diego, CA; ACM: New York, available on CD ROM
    • Hao, M.-H.; Scheraga, H. A. Supercomputing '95, Proceedings of the 1995 ACM/IEE Supercomputing Conference, December 3-8, 1995, San Diego, CA; ACM: New York, 1995; available on CD ROM.
    • (1995) Supercomputing '95
    • Hao, M.-H.1    Scheraga, H.A.2
  • 41
  • 45
    • 85033040986 scopus 로고    scopus 로고
    • note
    • The concave extent of the entropy curve is the primary statistical-mechanical criterion for the cooperativity of the folding transition. The sigmoidal shape of the thermal folding/unfolding curve, on the other hand, is only a secondary measure that does not provide a clear indication as to whether there is a free-energy barrier in the collapse transition of heteropolymers.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.