Nuclear spin relaxation rates associated with cross-correlated, dipole-dipole interactions are enlisted to help characterize the solution state dynamics of a small heptapeptide, deltorphin-I. A simple two-site jump model can be used to interpret the data obtained on two specific C-13 labeled residues, D-alanine and glycine. The influence of temperature and solvent upon the observed dynamics is investigated. Similarly, relaxation rates associated with dipole-shielding anisotropy interferences are used to examine the magnitude and orientation of various chemical shielding tensors within the D-alanine and glycine residues.