Chemical tools for membrane protein structural biology

被引:12
|
作者
Zhang, Qinghai [1 ]
Cherezov, Vadim [2 ]
机构
[1] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA
[2] Univ Southern Calif, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA
基金
美国国家卫生研究院;
关键词
PHOSPHOLIPID-BILAYER NANODISCS; SIZE-EXCLUSION CHROMATOGRAPHY; CRYSTAL-STRUCTURE; FACIAL AMPHIPHILES; BINDING-SITE; CRYSTALLIZATION; SOLUBILIZATION; STABILIZATION; MOLECULE; SYSTEM;
D O I
10.1016/j.sbi.2019.06.002
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
Solving high-resolution structures of membrane proteins has been an important challenge for decades, still lagging far behind that of soluble proteins even with the recent remarkable technological advances in X-ray crystallography and electron microscopy. Central to this challenge is the necessity to isolate and solubilize membrane proteins in a stable, natively folded and functional state, a process influenced by not only the proteins but also their surrounding chemical environment. This review highlights recent community efforts in the development and characterization of novel membrane agents and ligand tools to stabilize individual proteins and protein complexes, which together have accelerated progress in membrane protein structural biology.
引用
收藏
页码:278 / 285
页数:8
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