Downhill protein folding: evolution meets physics

被引：111

作者：

Gruebele, M ^{[1
]}

机构：

[1] Univ Illinois, Dept Chem, Urbana, IL 61801 USA

[2] Univ Illinois, Dept Phys, Urbana, IL 61801 USA

[3] Univ Illinois, Ctr Biophys & Computat Biol, Urbana, IL 61801 USA

来源：

COMPTES RENDUS BIOLOGIES | 2005年 / 328卷 / 08期

关键词：

protein function; temperature jump; hydrophobicity; activation barrier;

D O I：

10.1016/j.crvi.2005.02.007

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Proteins can be redesigned to fold downhill on a free energy surface characterized by only a few coordinates, confirming a principal prediction of the 'energy-landscape' model. Nonetheless, natural proteins have small but significant barriers. Spectroscopy and kinetics reveal potential biological causes for activation barriers during protein folding: evolution against protein aggregation and for protein function.

引用

收藏

页码：701 / 712

页数：12

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