| Literature DB >> 15317997 |
Guang Zhu1, Youlin Xia, Donghai Lin, Xiaolian Gao.
Abstract
Transverse relaxation-optimized spectroscopy (TROSY)-based nuclear magnetic resonance (NMR) experiments can be exploited to obtain chemical shift assignment and values of J-coupling constants, residual dipolar couplings, and nuclear Overhauser effects (NOEs) for structural studies of proteins, as discussed in Chapter 5. Furthermore, the application of TROSY-based NMR experiments can be extended to the measurements of molecule dynamics, amide proton exchange rates, and hydrogen bonds. This chapter describes these experiments.Entities:
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Year: 2004 PMID： 15317997 DOI： 10.1385/1-59259-809-9:161
Source DB: PubMed Journal: Methods Mol Biol ISSN： 1064-3745