The use of 2H, 13C, 15N multidimensional NMR to study the structure and dynamics of proteins

被引：479
作者：
Gardner, KH
Kay, LE
机构：
[1] Univ Toronto, Prot Engn Network Ctr Excellence, Toronto, ON M5S 1A8, Canada
[2] Univ Toronto, Dept Med Genet & Microbiol, Toronto, ON M5S 1A8, Canada
[3] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
[4] Univ Toronto, Dept Chem, Toronto, ON M5S 1A8, Canada
来源：
ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE | 1998年 / 27卷
关键词：
protein deuteration; triple resonance NMR; amino acid-specific isotopic labeling; structure determination; sidechain dynamics;
D O I：
10.1146/annurev.biophys.27.1.357
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：
During the past thirty years, deuterium labeling has been used to improve the resolution and sensitivity of protein NMR spectra used in a wide variety of applications. Most recently, the combination of triple resonance experiments and H-2, C-13, N-15 labeled samples has been critical to the solution structure determination of several proteins with molecular weights on the order of 30 kDa. Here we review the developments in isotopic labeling strategies, NMR pulse sequences, and structure-determination protocols that have facilitated this advance and hold promise for future NMR-based structural studies of even larger systems. As well, we detail recent progress in the use of solution H-2 NMR methods to probe the dynamics of protein sidechains.
引用
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页码：357 / 406
页数：50
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