Identifying the protein folding nucleus using molecular dynamics

被引：125

作者：

Dokholyan, NV

Buldyrev, SV

Stanley, HE

Shakhnovich, EI ^{[1
]}

机构：

[1] Boston Univ, Ctr Polymer Studies, Dept Phys, Boston, MA 02215 USA

[2] Harvard Univ, Dept Chem & Biol Chem, Cambridge, MA 02138 USA

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2000年 / 296卷 / 05期

关键词：

protein folding; kinetics; molecular dynamics; nucleus; transition state;

D O I：

10.1006/jmbi.1999.3534

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：

Molecular dynamics simulations of folding in an off-lattice protein model reveal a nucleation scenario, in which a few well-defined contacts are formed with high probability in the transition state ensemble of conformations. Their appearance determines folding cooperativity and drives the model protein into its folded conformation. Amino acid residues participating in those contacts may serve as "accelerator pedals" used by molecular evolution to control protein folding rate. (C) 2000 Academic Press.

引用

页码：1183 / 1188

页数：6

共 27 条

[1] NON-INTERACTING LOCAL-STRUCTURE MODEL OF FOLDING AND UNFOLDING TRANSITION IN GLOBULAR-PROTEINS .2. APPLICATION TO TWO-DIMENSIONAL LATTICE PROTEINS [J].