Please use this identifier to cite or link to this item: https://doi.org/10.1023/A:1025884922203
Title: Measurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins
Authors: Liu, W. 
Zheng, Y. 
Cistola, D.P.
Yang, D. 
Keywords: Cross-correlated relaxation
Fatty acid binding protein
Methyl dynamics
Order parameter
Issue Date: Dec-2003
Citation: Liu, W., Zheng, Y., Cistola, D.P., Yang, D. (2003-12). Measurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins. Journal of Biomolecular NMR 27 (4) : 351-364. ScholarBank@NUS Repository. https://doi.org/10.1023/A:1025884922203
Abstract: An understanding of side chain motions in protein is of great interest since side chains often play an important role in protein folding and intermolecular interactions. A novel method for measuring the dynamics of methyl groups in uniformly 13C-, 15N-labeled proteins has been developed by our group. The method relies on the difference in peak intensities of 13C quartet components of methyl groups, in a spectrum recording the free evolution of 13C under proton coupling in a constant-time period. Cross-correlated relaxation rates between 13C-1 H dipoles can be easily measured from the intensities of the multiplet components. The degree of the methyl restrictions (S′2) can be estimated from the cross-correlated relaxation rate. The method is demonstrated on a sample of human fatty acid binding protein in the absence of fatty acid. We obtained relaxation data for 33 out of 46 residues having methyl groups in apo-IFABP. It has been found that the magnitude of the CSA tensor of spin 13C in a methyl group could be estimated from the intensities of the 13C multiplet components.
Source Title: Journal of Biomolecular NMR
URI: http://scholarbank.nus.edu.sg/handle/10635/102484
ISSN: 09252738
DOI: 10.1023/A:1025884922203
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