Specific 12CβD212CγD2S13CεHD2 Isotopomer Labeling of Methionine To Characterize Protein Dynamics by 1H and 13C NMR Relaxation Dispersion

Abstract

Protein dynamics on the micro- to millisecond time scale is increasingly found to be critical for biological function, as demonstrated by numerous NMR relaxation dispersion studies. Methyl groups are excellent probes of protein interactions and dynamics because of their favorable NMR relaxation properties, which lead to sharp signals in the (1)H and (13)C… (More)
DOI: 10.1021/ja309294u

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@inproceedings{Weininger2012Specific1I, title={Specific 12CβD212CγD2S13CεHD2 Isotopomer Labeling of Methionine To Characterize Protein Dynamics by 1H and 13C NMR Relaxation Dispersion}, author={Ulrich Weininger and Zhihong Liu and Deane D. McIntyre and Hans J. Vogel and Mikael Akke}, booktitle={Journal of the American Chemical Society}, year={2012} }