OPTIMAL LOCAL PROPENSITIES FOR MODEL PROTEINS

被引：56
作者：
GOVINDARAJAN, S
GOLDSTEIN, RA
机构：
[1] UNIV MICHIGAN,DEPT CHEM,ANN ARBOR,MI 48109
[2] UNIV MICHIGAN,DIV BIOPHYS RES,ANN ARBOR,MI 48109
来源：
PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1995年 / 22卷 / 04期
关键词：
PROTEIN FOLDING; LATTICE MODELS; PROTEIN ENERGETICS; LOCAL INTERACTIONS; SPIN-GLASS THEORY;
D O I：
10.1002/prot.340220411
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Lattice models of proteins were used to examine the role of local propensities in stabilizing the native state of a protein, using techniques drawn from spin-glass theory to characterize the free-energy landscapes, In the strong evolutionary limit, optimal conditions for folding are achieved when the contributions from local interactions to the stability of the native state is small, Further increasing the local interactions rapidly decreases the foldability. (C) 1995 Wiley-Liss, Inc.
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收藏
页码：413 / 418
页数：6
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