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. 1970 May;66(1):111–116. doi: 10.1073/pnas.66.1.111

Secondary Structure of the Cyclic Moiety of the Peptide Hormone Oxytocin and Its Deamino Analog*

D W Urry 1,2,3,†, M Ohnishi 1,2,3,‡, Roderich Walter 1,2,3,‡,§
PMCID: PMC286095  PMID: 5273889

Abstract

The secondary structure of the cyclic moiety of oxytocin and deamino-oxytocin has been determined by nuclear magnetic resonance spectroscopy (220 MHz). Oxytocin, in a dimethylsulfoxide-methanol mixture, contains a β-turn involving the sequence -L-tyrosyl-L-isoleucyl-L-glutaminyl-L-asparaginyl-. Deamino-oxytocin, in addition to the β-turn, contains a hydrogen bond involving the amide hydrogen of the tyrosine residue and the peptide carbonyl group of the asparagine residue, resulting in an antiparallel β-type conformation for the ring component. An initial attempt has been made to relate conformational features of the hormonal peptides to their biological activity.

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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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