Folding scene investigation: membrane proteins

被引:66
|
作者
Booth, Paula J. [1 ]
Curnow, Paul [1 ]
机构
[1] Univ Bristol, Dept Biochem, Bristol BS8 1TD, Avon, England
基金
英国生物技术与生命科学研究理事会;
关键词
POTASSIUM CHANNEL KCSA; IN-VITRO; TRANSMEMBRANE HELICES; UNFOLDING PATHWAYS; DETERGENT MIXTURES; LIPID-COMPOSITION; ENERGY LANDSCAPE; RETINAL BINDING; POINT MUTATIONS; BACTERIORHODOPSIN;
D O I
10.1016/j.sbi.2008.12.005
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
Investigations into protein folding have concentrated on experimentally tractable proteins with the result that membrane protein folding remains unsolved. New evidence is providing insight into the nature of the interactions stabilising the folded state of (x-helical membrane proteins as well as giving hints on the character of the folding transition state. These developments show that classical methods used for water-soluble proteins can be successfully adapted for membrane proteins. The advances, coupled with increasing numbers of solved crystal structures, augur well for future research into the mechanisms of membrane protein folding.
引用
收藏
页码:8 / 13
页数:6
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