Helical membrane protein conformations and their environment

被引:55
|
作者
Cross, Timothy A. [1 ,2 ,3 ]
Murray, Dylan T. [2 ,3 ]
Watts, Anthony [4 ]
机构
[1] Florida State Univ, Dept Chem & Biochem, Tallahassee, FL 32306 USA
[2] Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA
[3] Florida State Univ, Natl High Magnet Field Lab, Tallahassee, FL 32310 USA
[4] Univ Oxford, Biomembrane Struct Unit, Dept Biochem, Oxford OX1 3QU, England
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2013年 / 42卷 / 10期
基金
英国医学研究理事会; 英国工程与自然科学研究理事会; 美国国家科学基金会;
关键词
Membrane proteins; Solid-state NMR; Lipids; Membrane protein crystallography; SOLID-STATE NMR; NUCLEAR-MAGNETIC-RESONANCE; M2 PROTON CHANNEL; PHOSPHOLIPID-BILAYER NANODISCS; LATERAL PRESSURE PROFILE; LIPID-BILAYER; CRYSTAL-STRUCTURE; SPIN-LABEL; X-RAY; ELECTRON CRYSTALLOGRAPHY;
D O I
10.1007/s00249-013-0925-x
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Evidence that membrane proteins respond conformationally and functionally to their environment is growing. Structural models, by necessity, have been characterized in preparations where the protein has been removed from its native environment. Different structural methods have used various membrane mimetics that have recently included lipid bilayers as a more native-like environment. Structural tools applied to lipid bilayer-embedded integral proteins are informing us about important generic characteristics of how membrane proteins respond to the lipid environment as compared with their response to other nonlipid environments. Here, we review the current status of the field, with specific reference to observations of some well-studied alpha-helical membrane proteins, as a starting point to aid the development of possible generic principles for model refinement.
引用
收藏
页码:731 / 755
页数:25
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