The longitudinal (T 1), transverse (T 2), and singlet state (T s) relaxation times of the geminal backbone protons (CH2) of L-Leu-Gly-Gly were studied by NMR spectroscopy at 9.4 T in a bovine hide gelatin gel composed in D2O at 25 °C. Gelatin granules were dissolved in a hot solution of the tripeptide and then the solution was allowed to gel inside a flexible silicone tubing. With increases in gelatin content, the T 2 and T s of the CH2 protons correspondingly decreased (T s/T 2 ~ constant), while the change in T 1 was relatively small. The largest observed T s/T 1 value was 3.3 at 46% w/v gelatin that was the lowest gelatin content examined. Stretching the tubing, and hence the gel, brought about anisotropic alignment of the constituents resulting in residual quadrupolar splitting of the resonance from D2O in (2)H NMR spectra, and residual dipolar splitting of the CH2 resonance in (1)H NMR spectra. WALTZ-16 decoupling during the relaxation intervals extended the singlet state relaxation time, but the efficacy diminished as the gels were stretched. Theoretically predicted T 1, T 2, and T s values, assuming intramolecular dipolar coupling as the only source of relaxation, were within the same order of magnitude as the experimentally observed values. Overall we showed that it is possible to observe a long-lived spin state in an anisotropic medium when T 2 is shorter than T 1 in the presence of non-zero residual dipolar couplings.