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- W2071556057 abstract "Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100 kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is provided in a study of malate synthase G, a 723 residue enzyme that has been a focal point of research efforts in my laboratory. Details of the labeling schemes that have been employed and optimal experiments for extraction of structural and dynamics information on this protein are described. NMR studies of protein dynamics, in principle, give insight into the relation between motion and function. A description of deuterium-based spin relaxation methods for the investigation of side chain dynamics is provided. Examples where millisecond (ms) time scale dynamics play an important role and where relaxation dispersion NMR spectroscopy has been particularly informative, including applications involving the membrane enzyme PagP and mutants of the Fyn SH3 domain that fold on a ms time scale, are presented." @default.
- W2071556057 created "2016-06-24" @default.
- W2071556057 creator A5076875040 @default.
- W2071556057 date "2005-04-01" @default.
- W2071556057 modified "2023-10-16" @default.
- W2071556057 title "NMR studies of protein structure and dynamics" @default.
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- W2071556057 doi "https://doi.org/10.1016/j.jmr.2004.11.021" @default.
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- W2071556057 hasPublicationYear "2005" @default.
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