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. 1972 Aug;69(8):2169–2173. doi: 10.1073/pnas.69.8.2169

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

P H Von Dreele *, A I Brewster †, J Dadok ‡, H A Scheraga *, F A Bovey †, M F Ferger *, V Du Vigneaud *
PMCID: PMC426893  PMID: 4506086

Abstract

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-CαH and CαH-CβH decoupling experiments. The conformation of lysine-vasopressin in water differs from its conformation in dimethylsulfoxide.

Keywords: proton assignments, dimethylsulfoxide, peptide, conformation, amino acids

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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