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NMR conformational studies on a synthetic peptide reproducing the [1‐20] processing domain of the pro‐ocytocin‐neurophysin precursor
Author(s) -
Falcigno Lucia,
Paolillo Livio,
D'Auria Gabriella,
Saviano Michele,
Simonetti Mario,
Di Bello Carlo
Publication year - 1996
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(199612)39:6<837::aid-bip8>3.0.co;2-w
Subject(s) - chemistry , neurophysins , peptide , ring (chemistry) , domain (mathematical analysis) , molecule , stereochemistry , peptide bond , molecular dynamics , biochemistry , computational chemistry , organic chemistry , mathematical analysis , mathematics , hormone
The combined use of several nuclear magnetic resonance and restrained molecular dynamics techniques allowed the formulation of a molecular model for the preferred solution conformation of a synthetic peptide reproducing the [1‐20] processing domain of the pro‐ocytocin‐neurophysin precursor. In the model, the conformation of the 20‐membered tocin ring, with the two Cys 1 and Cys 6 residues bridged by a disulphide bond, is very close to that observed for isolated ocytocin in the solid state; in addition, a type II β‐turn is postulated for the 7‐10 segment of the acyclic tail containing the Lys 11 ‐Arg 12 processing site, and connecting ocytocin to the neurophysin domain, while the C‐terminal 13‐20 segment of the molecule is believed to assume a helical structure. This particular structural organization could be important in participating as the favorable conformation for optimal substrate‐enzyme active site recognition and processing by specific endoproteases. © 1996 John Wiley & Sons, Inc.