Loop-closure principles in protein folding

被引：20

作者：

Weikl, Thomas R. ^{[1
]}

机构：

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

来源：

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS | 2008年 / 469卷 / 01期

关键词：

protein folding kinetics; native-state topology; two-state proteins; folding rates; contact order; topological measures; folding routes; loop-closure entropy; effective contact order;

D O I：

10.1016/j.abb.2007.06.018

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：

Simple theoretical concepts and models have been helpful to understand the folding rates and routes of single-domain proteins. As reviewed in this article, a physical principle that appears to underly these models is loop closure. (C) 2007 Elsevier Inc. All rights reserved.

引用

页码：67 / 75

页数：9

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