Folding α-helical membrane proteins:: kinetic studies on bacteriorhodopsin
被引:34
作者:
Booth, PJ
论文数: 0引用数: 0
h-index: 0
机构:
Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AY, EnglandUniv London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AY, England
Booth, PJ
[1
]
机构:
[1] Univ London Imperial Coll Sci Technol & Med, Dept Biochem, London SW7 2AY, England
来源:
FOLDING & DESIGN
|
1997年
/
2卷
/
06期
基金:
英国惠康基金;
关键词:
D O I:
10.1016/S1359-0278(97)00045-X
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 correct folding and assembly of proteins within biological membranes is essential for membrane biogenesis and function. In contrast to the large body of work on water-soluble protein folding, however, very little is known about how membrane proteins fold to their final structures. Recent biophysical studies on membrane-protein folding in vitro are beginning to shed light on this problem. In particular, the forces that the membrane lipids impose on the folding protein appear to control certain events. The seven-helix transmembrane protein bacteriorhodopsin has been the focus of much attention and kinetic studies on the folding of this protein form the basis of this review.