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PNAS | May 15, 1970 | vol. 66 | no. 1 | 111-116
Copyright © 1970 by the National Academy of Sciences

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

D. W. Urry, M. Ohnishi, and Roderich Walter

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 ß -turn involving the sequence -L-tyrosyl-L-isoleucyl-L-glutaminyl-L-asparaginyl-. Deamino-oxytocin, in addition to the ß -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 ß -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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