Nuclear magnetic resonance studies on the structure of the tetrapeptide tuftsin, L-threonyl-L-lysyl-L-prolyl-L-arginine, and its pentapeptide analogue L-threonyl-L-lysyl-L-prolyl-L-prolyl-L-arginine.
Nuclear magnetic resonance spectroscopy has been used to investigate the solution conformation of tuftsin, threonyllysylprolylarginine, as well as a pentapeptide inhibitor of tuftsin, threonyllysylprolylprolylarginine. Both proton and carbon-13 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, however, appear to be such that a normal 4 leads to 1 beta turn exists.
D006863:Hydrogen-Ion Concentration; D007128:Immunoglobulin Fragments; D009682:Magnetic Resonance Spectroscopy; D009842:Oligopeptides; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014405:Tuftsin
D007128:Immunoglobulin Fragments; D009842:Oligopeptides; D014405:Tuftsin