Flexible membrane proteins: functional dynamics captured by mass spectrometry

被引:19
作者
Zhou, Min [1 ]
Robinson, Carol V. [2 ]
机构
[1] Nanjing Univ Sci Technol, Inst Chem Biol & Adv Mat, Nanjing 210094, Jiangsu, Peoples R China
[2] Univ Oxford, Dept Chem, Phys & Theoret Chem Lab, Oxford OX1 3QZ, England
基金
英国惠康基金; 中国国家自然科学基金;
关键词
CRYSTAL-STRUCTURE; ATP SYNTHASE; CONFORMATIONAL-CHANGES; MULTIDRUG-RESISTANCE; STRUCTURAL DYNAMICS; ALTERNATING ACCESS; HYDROGEN-EXCHANGE; ESCHERICHIA-COLI; ABC TRANSPORTER; CROSS-LINKING;
D O I
10.1016/j.sbi.2014.08.005
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 are flexible molecular machines, responsible for the exchange of molecules in and out of the cell, which have evolved to perform specific and complex tasks with great efficiency. Obtaining accurate descriptions of their dynamics in the context of their function represents a major challenge for structural biology. Here we chart recent developments in mass spectrometry designed to characterize changes in the dynamics of membrane proteins in response to ligand binding or post-translational modifications. We focus on cooperative movements and structural changes across a range of timescales, from milliseconds to minutes, and highlight the contributions of mass spectrometry to our understanding of molecular mechanisms of diverse transmembrane processes.
引用
收藏
页码:122 / 130
页数:9
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