Probing Protein Side Chain Dynamics Via 13C NMR Relaxation

Protein side chain dynamics is associated with protein stability, folding, and intermolecular interactions. Detailed dynamics information is crucial for the understanding of protein function and biochemical and biophysical properties, which can be obtained using NMR relaxation techniques. In this review, 13C relaxation of methine, methylene and methyl groups with and without 1H decoupling are described briefly for a better understanding of how spin relaxation is associated with motional (dynamics) parameters. Developments in the measurement and interpretation of 13C autorelaxation and cross-correlated relaxation data are presented too. Finally, recent progress in the use of 13C relaxation to probe the dynamics of protein side chains is detailed mainly for the dynamics of non-deuterated proteins on picosecondnanosecond timescales.