Entropic barriers, frustration, and order: Basic ingredients in protein folding

被引：24

作者：

Camacho, CJ

机构：

[1] Facultad de Física, P. Universidad Católica de Chile, Santiago

来源：

PHYSICAL REVIEW LETTERS | 1996年 / 77卷 / 11期

关键词：

D O I：

10.1103/PhysRevLett.77.2324

中图分类号：

O4 [物理学];

学科分类号：

0702 ;

摘要：

We consider the intrinsic entropy and energy barriers of cross-linking in a set of M monomers, plus minimal kinetic restrictions on the folding process of a proteinlike molecule. For a finite-size chain, there is an effective folding transition to an ordered structure. Without frustration, this state is reached in a time that scales as M(lambda). with lambda similar or equal to 3. This scaling is limited by the amount of frustration which leads to the dynamical selectivity of proteins in a well defined range of temperatures, and M less than or similar to 300 monomers. These predictions resemble generic properties of in live globular proteins.

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页码：2324 / 2327

页数：4

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