Cooperativity and stability in a Langevin model of proteinlike folding

被引：19

作者：

Berriz, GF ^{[1
]}

Gutin, AM ^{[1
]}

Shakhnovich, EI ^{[1
]}

机构：

[1] HARVARD UNIV,DEPT CHEM & BIOL CHEM,CAMBRIDGE,MA 02138

来源：

JOURNAL OF CHEMICAL PHYSICS | 1997年 / 106卷 / 22期

关键词：

D O I：

10.1063/1.474039

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

We present two simplified models of protein dynamics based on Langevin's equation of motion in a viscous medium. We explore the effect of the potential energy function's symmetry on the kinetics and thermodynamics of simulated folding. We find that an isotropic potential energy function produces, at best, a modest degree of cooperativity. In contrast, a suitable anisotropic potential energy function delivers strong cooperativity. (C) 1997 American Institute of Physics.

引用

页码：9276 / 9285

页数：10

共 30 条

[1] IMPACT OF LOCAL AND NONLOCAL INTERACTIONS ON THERMODYNAMICS AND KINETICS OF PROTEIN-FOLDING [J].