Abstract
The peaks in the proton nuclear magnetic resonance spectrum of deamino-lysine-vasopressin in aqueous solution at pH values between 3 and 5 were assigned to particular amino-acid residues by use of the results of transfer-of-saturation studies, NH-C(alpha)H and C(alpha)H-C(beta)H decoupling experiments, and other data. The conformation of deamino-lysine-vasopressin in water differs from that of lysine-vasopressin in the same solvent.