Unravelling the folding of bacteriorhodopsin

被引:53
作者
Booth, PJ
机构
[1] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England
[2] Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AZ, England
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2000年 / 1460卷 / 01期
基金
英国生物技术与生命科学研究理事会;
关键词
bacteriorhodopsin; protein folding; membrane protein; membrane lipid; lateral pressure;
D O I
10.1016/S0005-2728(00)00125-0
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
The folding mechanism of integral membrane proteins has eluded detailed study, largely as a result of the inherent difficulties in folding these proteins in vitro. The seven-transmembrane helical protein bacteriorhodopsin has, however, allowed major advances to be made, not just on the folding of this particular protein, but also on the factors governing folding of transmembrane alpha-helical proteins in general. This review focusses on kinetic and equilibrium studies of bacteriorhodopsin folding in vitro. It covers what is currently known about secondary and tertiary structure formation as well as the events accompanying retinal binding, for protein in detergent and lipid systems, including native membrane samples. (C) 2000 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:4 / 14
页数:11
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