Measurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins - PubMed (original) (raw)

Measurement of methyl 13C-1H cross-correlation in uniformly 13C-, 15N-, labeled proteins

Weidong Liu et al. J Biomol NMR. 2003 Dec.

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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