Nuclear magnetic resonance studies on the structure of the tetrapeptide tuftsin L-threonyl-L-lysyl-L-prolyl-L-arginine, and its pentapeptide analog L-threonyl-L-lysyl-L-prolyl-L-prolyl-L-arginine

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Abstract
NMR spectroscopy was used to investigate the solution conformation of tuftsin, threonyllysylprolylarginine, and a pentapeptide inhibitor of tuftsin, threonyllysylprolylprolylarginine. Both 1H and 13C studies were performed. In water, neither peptide gives evidence of a preferred conformation. In dimethyl-d6 sulfoxide, tuftsin appears to prefer a particular conformation but the inhibitor does not. The conformation of tuftsin is one in which the amide NH proton of arginine is solvent shielded. The conformation does not appear to be such that a normal 4 .fwdarw. 1 .beta. turn exists.