Experimental approaches for NMR studies of side-chain dynamics in high-molecular-weight proteins

被引：53
|
作者：
Sheppard, Devon [1 ]
Sprangers, Remco [2 ]
Tugarinov, Vitali [1 ]
机构：
[1] Univ Maryland, Dept Chem & Biochem, College Pk, MD 20742 USA
[2] Max Planck Inst Dev Biol, D-72076 Tubingen, Germany
来源：
PROGRESS IN NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY | 2010年 / 56卷 / 01期
关键词：
Side-chain dynamics; NMR of large proteins; Selective isotope labeling; Methyl-TROSY; Spin relaxation; NUCLEAR-MAGNETIC-RESONANCE; MALATE-SYNTHASE-G; TIME-SCALE DYNAMICS; CHARACTERIZING CHEMICAL-EXCHANGE; HETERONUCLEAR TRANSVERSE RELAXATION; OPTIMIZED SPECTROSCOPY TROSY; CROSS-CORRELATED RELAXATION; DEUTERIUM SPIN PROBES; METHYL-GROUP DYNAMICS; MODEL-FREE APPROACH;
D O I：
10.1016/j.pnmrs.2009.07.004
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
A study was conducted to demonstrate experimental approaches for nuclear magnetic resonance (NMR) studies of side-chain dynamics in high-molecular-weight proteins. The investigations emphasized on spectroscopic NMR approaches and associated isotope labeling strategies that made such large protein assemblies amenable to quantitative NMR studies. The delay elements in NMR pulse-schemes were selected without concern about evolution due to 13C-13C one-bond scalar couplings, leading to improvements in sensitivity. The methyl-selective 13C enrichment was possible through the use of [12C, 2H]-labeled glucose as the main carbon source in minimal media for protein production.
引用
收藏
页码：1 / 45
页数：45
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