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The peaks in the proton NMR spectrum of lysine-vasopressin in aqueous solution at pH 3-5 were assigned to particular amino-acid residues by the use of the results of dilution studies and NH-C(alpha)H and C(alpha)H-C(beta)H decoupling experiments. The conformation of lysine-vasopressin in water differs from its conformation in dimethylsulfoxide.

Nuclear Magnetic Resonance Spectrum of Lysine-Vasopressin in Aqueous Solution and Its Structural Implications