Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR

被引：62

作者：

Hong, Mei ^{[1
]}

机构：

[1] Iowa State Univ, Dept Chem, Ames, IA 50011 USA

来源：

STRUCTURE | 2006年 / 14卷 / 12期

关键词：

D O I：

10.1016/j.str.2006.10.002

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：

Solid-state NMR is a versatile and powerful tool for determining the dynamic structure of membrane proteins at atomic resolution. I review the recent progress in determining the orientation, the internal and global protein dynamics, the oligomeric structure, and the ligand-bound structure of membrane proteins with both alpha-helical and beta sheet conformations. Examples are given that illustrate the insights into protein function that can be gained from the NMR structural information.

引用

收藏

页码：1731 / 1740

页数：10

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