Advances in solid-state NMR of membrane proteins

被引:11
|
作者
Wylie, Benjamin J. [1 ]
Do, Hoa Q. [1 ]
Borcik, Collin G. [1 ]
Hardy, Emily P. [1 ]
机构
[1] Texas Tech Univ, Dept Chem & Biochem, Lubbock, TX 79409 USA
基金
美国国家卫生研究院;
关键词
Solid-state NMR; membrane proteins; magic-angle spinning; structural biology; lipids; DYNAMIC-NUCLEAR-POLARIZATION; ANGLE-SPINNING NMR; M2 PROTON CHANNEL; MAGNETIC-RESONANCE-SPECTROSCOPY; ANABAENA SENSORY RHODOPSIN; INDUCED CONFORMATIONAL-CHANGES; RESISTANCE TRANSPORTER EMRE; CHEMICAL-SHIFT ASSIGNMENTS; CHIMERIC POTASSIUM CHANNEL; INFLUENZA-A;
D O I
10.1080/00268976.2016.1252470
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Solid-state nuclear magnetic resonance (SSNMR) is an NMR spectroscopy applied to condensed-phase systems, including membrane proteins. Membrane protein fold and function are dependent upon interactions with surrounding bilayer components. Structural and functional analyses are thus challenging, and newapproaches are needed to better characterise these systems. SSNMR is uniquely suited to the examination of membrane proteins in native environments, and has the capabilities to elucidate complex protein mechanisms and structures. Notable research implementing SSNMR is aimed at developing new strategies and technology to efficiently target membrane proteins within synthetic and biological membranes. Significant advances have been made: observation of protein function in native environments, emergence of in situ methods to examine integral proteins within natural membranes, sensitivity enhancement techniques and cutting-edge structure determination methods. We present how these advances are applied to answer outstanding questions in structural biology. Experiments have shown consistent results for protein investigations in biological membranes and synthetic lipid compositions, indicating that SSNMR is an innovative and direct approach for the study of these systems. [GRAPHICS] .
引用
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页码:3598 / 3609
页数:12
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