| Literature DB >> 21947927 |
Xinli Liao1, Raquel Godoy-Ruiz, Chenyun Guo, Vitali Tugarinov.
Abstract
A two-dimensional TROSY-based SIM-(13)C(m)-(1)H(m)/(1)H-(15)N NMR experiment for simultaneous measurements of methyl (1) D (CH) and backbone amide (1) D (NH) residual dipolar couplings (RDC) in {U-[(15)N,(2)H]; Ileδ1-[(13)CH(3)]; Leu,Val-[(13)CH(3)/(12)CD(3)]}-labeled samples of large proteins is described. Significant variation in the alignment tensor of the 82-kDa enzyme Malate synthase G is observed as a function of only slight changes in experimental conditions. The SIM-(13)C(m)-(1)H(m)/(1)H-(15)N data sets provide convenient means of establishing the alignment tensor characteristics via the measurement of (1) D (NH) RDCs in the same protein sample.Entities:
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Year: 2011 PMID: 21947927 DOI: 10.1007/s10858-011-9553-x
Source DB: PubMed Journal: J Biomol NMR ISSN: 0925-2738 Impact factor: 2.835