NMR Studies of Large Proteins

被引：56
|
作者：
Jiang, Yajun
Kalodimos, Charalampos G. [1 ]
机构：
[1] Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USA
来源：
JOURNAL OF MOLECULAR BIOLOGY | 2017年 / 429卷 / 17期
关键词：
large proteins; NMR spectroscopy; protein complexes; MOLECULAR-WEIGHT PROTEINS; ISOTOPE LABELING STRATEGIES; METHYL-GROUPS; BIOLOGICAL MACROMOLECULES; BETA(2)-ADRENERGIC RECEPTOR; CHAPERONE MACHINES; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; 20S PROTEASOME; C-13;
D O I：
10.1016/j.jmb.2017.07.007
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：
Recent breakthroughs in isotope-labeling and pulse sequence techniques have enabled the NMR characterization of large protein systems with molecular masses of hundreds of kilodaltons. NMR studies of a great variety of large proteins have provided unique insights into the binding, dynamic, and allosteric mechanisms. Here we present a brief summary of these developments by highlighting few cases that exemplify the uniqueness of NMR in providing atomic resolution information into key dynamic processes and structures of protein complexes with high degree of flexibility. (C) 2017 Elsevier Ltd. All rights reserved.
引用
收藏
页码：2667 / 2676
页数：10
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