C-13 CPMAS NMR has been investigated in application to protein samples with a variety of deuteration patterns. Samples were prepared with protons in either all hydrogen positions, only in the exchangeable sites, or in the exchangeable sites plus select methyl groups. CP dynamics, T-1 relaxation times, and C-13 line widths have been compared. Using ubiquitin as a model system, reasonable H-1-C-13 CP transfer is observed for the extensively deuterated samples. In the absence of deuterium decoupling, the C-13 line widths observed for the deuterated samples are identical to those observed for the perprotio samples with a MAS rate of 20 kHz. Extensive deuteration has little effect on the T-1 of the exchangeable protons. On the basis of these observations, it is clear that there are no substantive compromises accompanying the use of extensive deuteration in the design of H-1, N-15, or C-13 solid-state NMR methods.