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
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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