Mono- and bi-selective proton spin-lattice relaxation rates of L- and D-tryptophan have been measured in the free state and in the presence of human serum albumin; the selective relaxation rates of the amino acid are strongly enhanced in the presence of albumin and different values for the protons of the two antipodes in the bound state are observed.
G. Uccello-Barretta, E. Domenici, C. Bertucci and P. Salvadori, J. Chem. Soc., Chem. Commun., 1989, 1178 DOI: 10.1039/C39890001178
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