Cooperativity in two-state protein folding kinetics

被引：61

作者：

Weikl, TR ^{[1
]}

Palassini, M

Dill, KA

机构：

[1] Max Planck Inst Colloids & Interfaces, D-14424 Potsdam, Germany

[2] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA

来源：

PROTEIN SCIENCE | 2004年 / 13卷 / 03期

关键词：

protein folding kinetics; two-state folding; folding cooperativity; Phi-value analysis; effective contact order; loop-closure entropy; master equation;

D O I：

10.1110/ps.03403604

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：

We present a solvable model that predicts the folding kinetics of two-state proteins from their native structures. The model is based on conditional chain entropies. It assumes that folding processes are dominated by small-loop closure events that can be inferred from native structures. For C12, the src SH3 domain, TNfn3, and protein L, the model reproduces two-state kinetics, and it predicts well the average Phi-values for secondary structures. The barrier to folding is the formation of predominantly local structures such as helices and hairpins, which are needed to bring nonlocal pairs of amino acids into contact.

引用

页码：822 / 829

页数：8

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