Applications of solid-state NMR to membrane proteins

被引:54
作者
Ladizhansky, Vladimir [1 ,2 ]
机构
[1] Univ Guelph, Dept Phys, Guelph, ON N1G 2W1, Canada
[2] Univ Guelph, Biophys Interdept Grp, Guelph, ON N1G 2W1, Canada
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2017年 / 1865卷 / 11期
基金
加拿大自然科学与工程研究理事会;
关键词
Lipid bilayer; Cell membrane; Membrane protein; Protein structure; Solid-state NMR; Dynamic Nuclear Polarization; In situ solid-state NMR; DYNAMIC-NUCLEAR-POLARIZATION; SIDE-CHAIN PROTONS; RESONANCE ASSIGNMENT; PERDEUTERATED PROTEINS; PHOTOACTIVE SITE; PICHIA-PASTORIS; LABELED PROTEIN; SPECTROSCOPY; ANGLE; RESOLUTION;
D O I
10.1016/j.bbapap.2017.07.004
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
Membrane proteins mediate flow of molecules, signals, and energy between cells and intracellular compartments. Understanding membrane protein function requires a detailed understanding of the structural and dynamic properties involved. Lipid bilayers provide a native-like environment for structure-function investigations of membrane proteins. In this review we give a general discourse on the recent progress in the field of solid-state NMR of membrane proteins. Solid-state NMR is a variation of NMR spectroscopy that is applicable to molecular systems with restricted mobility, such as high molecular weight proteins and protein complexes, supramolecular assemblies, or membrane proteins in a phospholipid environment. We highlight recent advances in applications of solid-state NMR to membrane proteins, specifically focusing on the recent developments in the field of Dynamic Nuclear Polarization, proton detection, and solid-state NMR applications in situ (in cell membranes). This article is part of a Special Issue entitled: Biophysics in Canada, edited by Lewis Kay, John Baenziger, Albert Berghuis and Peter Tieleman.
引用
收藏
页码:1577 / 1586
页数:10
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