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

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

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

Prog Nucl Magn Reson Spectrosc. 2014 Feb;77:49-68

Authors: Tugarinov V

Abstract
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 (15)N and (13)C nuclei in (15)N-D and (13)C-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 ((15)N, (13)C, (1)H) is provided rather than those of deuterium itself.


PMID: 24411830 [PubMed - in process]



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