Membrane proteins shape up:: understanding in vitro folding

被引：48

作者：

Booth, Paula J. ^{[1
]}

Curnow, Paul ^{[1
]}

机构：

[1] Univ Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2006年 / 16卷 / 04期

基金：

英国惠康基金; 英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/j.sbi.2006.06.004

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：

Progress in structural biology has begun to reveal the precise architecture of integral membrane proteins. However, the manner in which these complex structures are achieved remains unclear. Recent developments are starting to shed light on the unfolding and folding of a small but growing number of membrane proteins. Mechanistic details derived from kinetic and thermodynamic experiments now enable comparison of the folding of different membrane proteins and their water-soluble cousins. This work also has important implications for other structural and functional studies of membrane proteins in vitro.

引用

页码：480 / 488

页数：9

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