An NMR experiment is presented for the measurement of the time scale of methyl side-chain dynamics in proteins that are labeled with methyl groups of the (13)CHD(2) variety. The measurement is accomplished by selecting a magnetization mode that to excellent approximation relaxes in a single-exponential manner with a T(1)-like rate. The combination of R(1)((13)CHD(2)) and R(2)((13)CHD(2)) (2)H relaxation rates facilitates the extraction of motional parameters from (13)CHD(2)-labeled proteins exclusively. The utility of the methodology is demonstrated with applications to proteins with tumbling times ranging from 2 ns (protein L, 7.5 kDa, 45 degrees C) to 54 ns (malate synthase G, 82 kDa, 37 degrees C); dynamics parameters are shown to be in excellent agreement with those obtained in (2)H NMR studies of other methyl isotopomers. A consistency relationship is found to exist between R(1)((13)CHD(2)) and the relaxation rates of pure longitudinal and quadrupolar order modes in (13)CH(2)D-labeled methyl groups, and experimental rates measured for a number of proteins are shown to be in excellent agreement with expectations based on theory. The present methodology extends the applicability of (2)H relaxation methods for the quantification of side-chain dynamics in high molecular weight proteins.