Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better

被引:94
作者
Poget, Sebastien F. [1 ]
Girvin, Mark E. [1 ]
机构
[1] Yeshiva Univ Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10461 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | 2007年 / 1768卷 / 12期
关键词
micelle; bicelle; structure; Smr; multidrug resistance;
D O I
10.1016/j.bbamem.2007.09.006
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
Considerable progress has been made recently on solution NMR studies of multi-transmembrane helix membrane protein systems of increasing size. Careful correlation of structure with function has validated the physiological relevance of these studies in detergent micelles. However, larger micelle and bicelle systems are sometimes required to stabilize the active forms of dynamic membrane proteins, such as the bacterial small multidrug resistance transporters. Even in these systems with aggregate molecular weights well over 100 kDa, solution NMR structural studies are feasible-but challenging. (C) 2007 Elsevier B.V. All rights reserved.
引用
收藏
页码:3098 / 3106
页数:9
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