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

Copyright © 2013 Elsevier B.V. All rights reserved.

Bibliographische Detailangaben
Veröffentlicht in:Progress in nuclear magnetic resonance spectroscopy. - 1998. - 77(2014) vom: 08. Feb., Seite 49-68
1. Verfasser: Tugarinov, Vitali (VerfasserIn)
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2014
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... Malate Synthase G NOE Protein backbone geometry Protein dynamics QCC RDC Spin relaxation in deuterium-containing spin-systems TROSY bilinear rotation decoupling chemical shift anisotropy nuclear Overhauser effect quadrupolar coupling constant residual dipolar coupling transverse relaxation optimized spectroscopy Proteins Solutions Deuterium AR09D82C7G
LEADER 01000caa a22002652 4500
001 NLM234360720
003 DE-627
005 20250216131612.0
007 cr uuu---uuuuu
008 231224s2014 xx |||||o 00| ||eng c
024 7 |a 10.1016/j.pnmrs.2013.08.001  |2 doi 
028 5 2 |a pubmed25n0781.xml 
035 |a (DE-627)NLM234360720 
035 |a (NLM)24411830 
035 |a (PII)S0079-6565(13)00077-0 
040 |a DE-627  |b ger  |c DE-627  |e rakwb 
041 |a eng 
100 1 |a Tugarinov, Vitali  |e verfasserin  |4 aut 
245 1 0 |a Indirect use of deuterium in solution NMR studies of protein structure and hydrogen bonding 
264 1 |c 2014 
336 |a Text  |b txt  |2 rdacontent 
337 |a ƒaComputermedien  |b c  |2 rdamedia 
338 |a ƒa Online-Ressource  |b cr  |2 rdacarrier 
500 |a Date Completed 31.08.2014 
500 |a Date Revised 13.01.2014 
500 |a published: Print-Electronic 
500 |a Citation Status MEDLINE 
520 |a Copyright © 2013 Elsevier B.V. All rights reserved. 
520 |a 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 
650 4 |a Journal Article 
650 4 |a Review 
650 4 |a BIRD 
650 4 |a CPMG 
650 4 |a CSA 
650 4 |a Carr–Purcell–Meiboom–Gill pulse train 
650 4 |a Deuteration 
650 4 |a Deuterium isotope shifts 
650 4 |a Hydrogen bonds 
650 4 |a MSG 
650 4 |a Malate Synthase G 
650 4 |a NOE 
650 4 |a Protein backbone geometry 
650 4 |a Protein dynamics 
650 4 |a QCC 
650 4 |a RDC 
650 4 |a Spin relaxation in deuterium-containing spin-systems 
650 4 |a TROSY 
650 4 |a bilinear rotation decoupling 
650 4 |a chemical shift anisotropy 
650 4 |a nuclear Overhauser effect 
650 4 |a quadrupolar coupling constant 
650 4 |a residual dipolar coupling 
650 4 |a transverse relaxation optimized spectroscopy 
650 7 |a Proteins  |2 NLM 
650 7 |a Solutions  |2 NLM 
650 7 |a Deuterium  |2 NLM 
650 7 |a AR09D82C7G  |2 NLM 
773 0 8 |i Enthalten in  |t Progress in nuclear magnetic resonance spectroscopy  |d 1998  |g 77(2014) vom: 08. Feb., Seite 49-68  |w (DE-627)NLM098212745  |x 1873-3301  |7 nnns 
773 1 8 |g volume:77  |g year:2014  |g day:08  |g month:02  |g pages:49-68 
856 4 0 |u http://dx.doi.org/10.1016/j.pnmrs.2013.08.001  |3 Volltext 
912 |a GBV_USEFLAG_A 
912 |a SYSFLAG_A 
912 |a GBV_NLM 
912 |a GBV_ILN_350 
951 |a AR 
952 |d 77  |j 2014  |b 08  |c 02  |h 49-68