期刊
JOURNAL OF MAGNETIC RESONANCE
卷 163, 期 1, 页码 92-98出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/S1090-7807(03)00105-8
关键词
TROSY; J-spectroscopy; scalar couplings; residual dipolar couplings; RNA; protein
资金
- NIGMS NIH HHS [GM59107] Funding Source: Medline
With the application of RDCs in high-resolution NMR studies of macromolecules, there has been an interest in the development of accurate, sensitive methods for measuring N-15-H-1 and C-13-H-1 one-bond coupling constants. Most methods for determining these couplings are based on the measurement of the displacement between cross-peak components in J-coupled spectra. However, for large macromolecules and macromolecular complexes, these methods are often unreliable since differential relaxation can significantly broaden one of the multiplet components (i.e., the anti-TROSY component) and thereby make accurate determination of its position difficult. To overcome this problem, a J-evolved transverse relaxation optimized (JE-TROSY) method is presented for the determination of one-bond couplings that involves J-evolution of the sharpest cross-peak multiplet component selected in a TROSY experiment. Couplings are measured from the displacement of the TROSY component in the additional J-evolution dimension relative to a zero frequency origin. The JE-TROSY method is demonstrated on uniformly labeled N-15,C-13-labeled RNA and peptide samples, as well as with an RNA-protein complex, in which the protein is uniformly N-15,C-13-labeled. In all cases, resolved, sensitive spectra are obtained from which heteronuclear one-bond J-couplings could be accurately and easily measured. Published by Elsevier Science (USA).
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