| Abstract: | Carbon-13 spin-lattice relaxation times have been measured in glycine and the tripeptide pro-leu-gly-NH2. These times are compared with those measured in the same compounds where the glycine α-carbon has been deuterated. In this manner evidence is obtained which indicates that mechanisms other than dipolar interactions with covalently bonded protons may contribute to carbon-13 spin-lattice relaxation. The effect of these additional mechanisms is found to be non-negligible for the carbonyl carbon of glycine and the glycine α-carbon of the tripeptide. The implication of these findings for deducing motional information from carbon-13 relaxation measurements is briefly discussed. |
