Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding

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• 作者：Vitali Tugarinov
• 关键词：TROSY ; transverse relaxation optimized spectroscopy ; BIRD ; bilinear rotation decoupling ; CPMG ; Carr&ndash ; Purcell&ndash ; Meiboom&ndash ; Gill pulse train ; QCC ; quadrupolar coupling constant ; CSA ; chemical shift anisotropy ; RDC ; residual dipolar coupling ; NOE ; nuclear Overhauser effect ; MSG ; Malate Synthase G
• 刊名：Progress in Nuclear Magnetic Resonance Spectroscopy
• 出版年：February, 2014
• 年：2014
• 卷：77
• 期：Complete
• 页码：49-68
• 全文大小：4756 K

文摘

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 鈥榠ndirect鈥?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.