Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding
Copyright © 2013 Elsevier B.V. All rights reserved.
| Veröffentlicht in: | Progress in nuclear magnetic resonance spectroscopy. - 1998. - 77(2014) vom: 08. Feb., Seite 49-68 |
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| 1. Verfasser: | |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2014
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| Zugriff auf das übergeordnete Werk: | Progress in nuclear magnetic resonance spectroscopy |
| Schlagworte: | Journal Article Review BIRD CPMG CSA Carr–Purcell–Meiboom–Gill pulse train Deuteration Deuterium isotope shifts Hydrogen bonds MSG mehr... |
| Zusammenfassung: | Copyright © 2013 Elsevier B.V. All rights reserved. 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 |
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| Beschreibung: | Date Completed 31.08.2014 Date Revised 13.01.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-3301 |
| DOI: | 10.1016/j.pnmrs.2013.08.001 |