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Volumn 106, Issue 22, 1997, Pages 9276-9285

Cooperativity and stability in a Langevin model of proteinlike folding

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0000019441     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.474039     Document Type: Article
Times cited : (19)

References (34)
  • 16
    • 85033278997 scopus 로고    scopus 로고
    • note
    • We have chosen to use the term "native" to designate the lowest-energy configuration, since, by design, our model proteins always fold towards the global energy minimum. This is not necessarily the case for all real proteins.
  • 18
    • 85033302064 scopus 로고    scopus 로고
    • note
    • Our choice of this function is quite arbitrary, since our immediate purpose here is to test the effects of the potential function's anisotropy and steric nucleation (see the Discussion section) on the cooperativity of the folding transition. For this purpose, all that is required of the test function is that (1) it have value 1 at θ=θ, and decay monotonically to 0 as θ→π; and (2) it be differentiable almost everywhere in the interval [0,π] (since we must be able to compute the gradient of the potential to get the resulting regular force). The function we chose decays rapidly to 0 as θ→π, but we have not studied the question of how steep this decay needs to be to yield the results we report here.
  • 21
    • 85033313329 scopus 로고    scopus 로고
    • note
    • α distance=3.8 Å, to make our results more directly comparable to experimental values.
  • 25
    • 85033314984 scopus 로고    scopus 로고
    • note
    • When comparing Figs. 3 and 8, it is important to be aware of the large difference between the time (abscissa) scales for the isotropic and the anisotropic models.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.