Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins
 

Simultaneous measurement of 1Hâ??15N and Methyl 1Hmâ??13Cm residual dipolar couplings in large proteins


Abstract A two-dimensional TROSY-based SIM-13Cmâ??1Hm/1Hâ??15N NMR experiment for simultaneous measurements of methyl 1 D CH and backbone amide 1 D NH residual dipolar couplings (RDC) in {U-[15N,2H]; Ileδ1-[13CH3]; Leu,Val-[13CH3/12CD3]}-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-13Cmâ??1Hm/1Hâ??15N data sets provide convenient means of establishing the alignment tensor characteristics via the measurement of 1 D NH RDCs in the same protein sample.

• Content Type Journal Article
• Category Article
• Pages 191-198
• DOI 10.1007/s10858-011-9553-x
• Authors
  • Xinli Liao, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA
  • Raquel Godoy-Ruiz, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA
  • Chenyun Guo, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA
  • Vitali Tugarinov, Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738
  • Journal Volume Volume 51
  • Journal Issue Volume 51, Numbers 1-2

Source: Journal of Biomolecular NMR