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Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding
Progress in Nuclear Magnetic Resonance Spectroscopy ( IF 7.3 ) Pub Date : 2014-02-01 , DOI: 10.1016/j.pnmrs.2013.08.001
Vitali Tugarinov 1
Affiliation  

A description of the utility of deuteration in protein NMR is provided with an emphasis on quantitative evaluation of the effects of deuteration on a number of NMR parameters of proteins: (1) chemical shifts, (2) scalar coupling constants, (3) relaxation properties (R1 and R2 rates) of nuclei directly attached to one or more deuterons as well as protons of methyl groups in a highly deuterated environment, (4) scalar relaxation of 15N and 13C nuclei in 15N-D and 13C-D spin systems as a measure of hydrogen bonding strength, and (5) NOE-based applications of deuteration in NMR studies of protein structure. The discussion is restricted to the 'indirect' use of deuterium in the sense that the description of NMR parameters and properties of the nuclei affected by nearby deuterons (15N, 13C, 1H) is provided rather than those of deuterium itself.

中文翻译:

在蛋白质结构和氢键的溶液核磁共振研究中间接使用氘

对氘化在蛋白质 NMR 中的应用进行了描述,重点是定量评估了氘化对蛋白质的许多 NMR 参数的影响:(1) 化学位移,(2) 标量耦合常数,(3) 弛豫特性(R1 和 R2 速率)直接连接到一个或多个氘核的原子核以及高度氘化环境中的甲基质子,(4)15N-D 和 13C-D 自旋系统中 15N 和 13C 原子核的标量弛豫氢键强度的测量,以及 (5) 基于 NOE 的氘化在蛋白质结构的 NMR 研究中的应用。讨论仅限于“间接”使用氘,因为提供了受附近氘核(15N、13C、1H)影响的核的 NMR 参数和性质的描述,而不是氘本身的描述。
更新日期:2014-02-01
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