Publication date: Available online 28 August 2013 Source:Progress in Nuclear Magnetic Resonance Spectroscopy
Author(s): Vitali Tugarinov
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 (R 1 and R 2 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. Graphical abstract
Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Molecular Hydrogen Tweezers: Structure and Mechanisms by Neutron Diffraction, NMR, and Deuterium Labeling Studies in Solid and Solution
Felix Schulz, Victor Sumerin, Sami Heikkinen, Bjo?rn Pedersen, Cong Wang, Michiko Atsumi, Markku Leskela?, Timo Repo, Pekka Pyykko?, Winfried Petry and Bernhard Rieger
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja206394w/aop/images/medium/ja-2011-06394w_0015.gif
Journal of the American Chemical Society
DOI: 10.1021/ja206394w
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Abstract:
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Indirect Use of Deuterium in Solution NMR Studies of Protein Structure and Hydrogen Bonding
Linear Mode
