Structure and Dynamics of Membrane Proteins by Magic Angle Spinning Solid-State NMR

被引:256
|
作者
McDermott, Ann [1 ]
机构
[1] Columbia Univ, Dept Chem, New York, NY 10027 USA
关键词
biological NMR; dynamics; membrane proteins; solid-state NMR; NUCLEAR-MAGNETIC-RESONANCE; 3D STRUCTURE DETERMINATION; CHEMICAL-SHIFT ASSIGNMENT; INDUCED CONFORMATIONAL-CHANGES; ESCHERICHIA-COLI THIOREDOXIN; SECONDARY STRUCTURE-ANALYSIS; CHIMERIC POTASSIUM CHANNEL; DISTANCE MEASUREMENTS; ROTATING SOLIDS; MICROCRYSTALLINE UBIQUITIN;
D O I
10.1146/annurev.biophys.050708.133719
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Membrane proteins remain difficult to study by traditional methods. Magic angle spinning solid-state NMR (MAS SSNMR) methods present an important lit approach for studying membrane proteins of moderate size. Emerging MAS SSNMR methods are based out extensive assignments of the nuclei as a basis for structure determination and characterization of function. These methods live already been used to characterize fibrils and globular proteins and are being increasingly used to study membrane proteins embedded in lipids. This review highlights recent applications to intrinsic membrane proteins and Summarizes recent technical advances that will enable these methods to be utilized for more complex membrane protein systems in the near future.
引用
收藏
页码:385 / 403
页数:19
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