Applications of Single-Molecule Methods to Membrane Protein Folding Studies

被引:26
|
作者
Jefferson, Robert E. [1 ]
Min, Duyoung [1 ]
Corin, Karolina [1 ]
Wang, Jing Yang [1 ]
Bowie, James U. [1 ]
机构
[1] Univ Calif Los Angeles, UCLA DOE Inst, Inst Mol Biol, Los Angeles, CA 90095 USA
基金
新加坡国家研究基金会;
关键词
TRANSMEMBRANE DOMAIN INTERACTIONS; RESONANCE ENERGY-TRANSFER; HELIX-HELIX INTERACTIONS; ENDOPLASMIC-RETICULUM; PLASMA-MEMBRANE; BIOLOGICAL MEMBRANE; FORCE SPECTROSCOPY; INHIBITOR BINDING; MASS-SPECTROMETRY; SEC61; TRANSLOCON;
D O I
10.1016/j.jmb.2017.05.021
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
Protein folding is a fundamental life process with many implications throughout biology and medicine. Consequently, there have been enormous efforts to understand how proteins fold. Almost all of this effort has focused on water-soluble proteins, however, leaving membrane proteins largely wandering in the wilderness. The neglect has occurred not because membrane proteins are unimportant but rather because they present many theoretical and technical complications. Indeed, quantitative membrane protein folding studies are generally restricted to a handful of well-behaved proteins. Single-molecule methods may greatly alter this picture, however, because the ability to work at or near infinite dilution removes aggregation problems, one of the main technical challenges of membrane protein folding studies. (C) 2017 Elsevier Ltd. All rights reserved.
引用
收藏
页码:424 / 437
页数:14
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