Measurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins |
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Authors: | Weidong Liu Yu Zheng David P. Cistola Daiwen Yang |
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Affiliation: | (1) Department of Biological Sciences and Department of Chemistry, National University of Singapore, 4 Science Drive, 117543, Singapore;(2) Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, 660 South Euclid Avenue, Campus Box 8231, St. Louis, MO, 63110, U.S.A |
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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-1H 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. |
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Keywords: | cross-correlated relaxation fatty acid binding protein methyl dynamics order parameter |
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