Secondary Structure of the Cyclic Moiety of the Peptide Hormone Oxytocin and Its Deamino Analog*
AUTOR(ES)
Urry, D. W.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=286095Documentos Relacionados
- Conformational Energy Studies of Oxytocin and Its Cyclic Moiety
- DEUTERATED OXYTOCINS: THE SYNTHESIS AND BIOLOGICAL PROPERTIES OF A CRYSTALLINE ANALOG OF DEAMINO-OXYTOCIN DEUTERATED IN THE 5-ASPARAGINE POSITION*
- A Neurohypophyseal Hormone Analog with Selective Oxytocin-Like Activities and Resistance to Enzymatic Inactivation: An Approach to the Design of Peptide Drugs*
- Surface properties of an amphiphilic peptide hormone and of its analog: corticotropin-releasing factor and sauvagine.
- The gene for the hypothalamic peptide hormone oxytocin is highly expressed in the bovine corpus luteum: biosynthesis, structure and sequence analysis.