It has been proposed several NMR methods to study sidechain dynamics in proteins. In one such approach, proteins are uniformly labeled with 13C (and/or 15N) and fractionally deuterated, allowing measurement of relaxation rates of deuterons in, for instance, CH2D and CHD2 systems. 2H relaxation is governed mainly by quadrupolar interaction and is insensitive to interactions with surrounding nuclei.

• Model selection for the interpretation of protein side chain methyl dynamics from ²H and ¹³C relaxation data (03JB325-25).
• Measurement of side-chain dynamics of methyl groups from ²H-based relaxation experiments ( 96BIO361 , 95JACS11536 , 97JB283 , 99JACS2891 , 99JB181-13 ). Applications have been reported to study the hydrophobic core packing ( 99JB135 ).
• ²H T₁ (C_zD_z) and ²H T_1ro (C_zD_y) of CHD methylene groups in ¹⁵N, ¹³C, and 50%-²H-labeled proteins ( 98JMB939-276 ).
• ¹³C T₁ and T₂ relaxation times in deuterated methylene carbon systems ( 93JACS11026 ).
• Measurement of ²H T₁ and T₁(ro) relaxation times at all methyl positions in fractionally ²H-labeled proteins ( 95JACS11536 ).
• Measurement of ²H relaxation rates in ¹H-¹⁵N-²H systems ( 97JACS3842 ).
• Measurement of ¹³CA T₁(ro) and T₂ relaxation times for ¹³CA-²H spin systems ( 94JACS11655 ).
•  Effects of cross correlation and cross relaxation on 2H relaxation methods ( 96JMRB213-110 ).
• Measurement of 1H and 13C relaxation rates of 13CHD2 isotopomers and 2H relaxation rates of 13CH2D isotopomers using a simple perdeuterated proteins. ( 01JACS6164 )
• New experiments to measure five relaxation rates in CH2D methyl groups in fractionally deuterated proteins and application to side-chain dynamics ( 02JACS6439 and 02JACS6449 )
• Side-chain dynamics in unfolded protein states ( 03JACS1748 )