Evidence for beta-turn structure in model peptides reproducing pro-ocytocin/neurophysin proteolytic processing site

Details

Serval ID
serval:BIB_BDFE11E93989
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Evidence for beta-turn structure in model peptides reproducing pro-ocytocin/neurophysin proteolytic processing site
Journal
Biochemical and Biophysical Research Communications
Author(s)
Rholam  M., Cohen  P., Brakch  N., Paolillo  L., Scatturin  A., Di Bello  C.
ISSN
0006-291X (Print)
Publication state
Published
Issued date
05/1990
Volume
168
Number
3
Pages
1066-73
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May 16
Abstract
The structural organization of small peptides reproducing the amino acid sequence of the common ocytocin/neurophysin precursor around the LysArg cleavage locus was investigated by a combination of spectroscopical techniques. In water both circular dichroism and [1H] NMR spectra indicated that these peptides adopted a random conformation. Evidence for folded structures was obtained when these compounds were placed in a membrane-like environment i.e. 40 mM SDS in phosphate buffer or trifluoroethanol. Whereas the CD spectra indicated the formation of various types of beta-turn in rapid equilibrium, measurements of NH temperature coefficients and Nuclear Overhauser Effects by 400 and 500 MHz NMR revealed the existence of contacts and of a folded conformation. These observations are discussed in relation with previous hypothesis made on the secondary structure organization of the proteolytic processing site of polypeptide hormone precursors.
Keywords
Amino Acid Sequence Circular Dichroism Magnetic Resonance Spectroscopy Models, Chemical Molecular Sequence Data Neurophysins/*metabolism Oligopeptides/*chemical synthesis/metabolism Oxytocin/*analogs & derivatives/metabolism Peptide Hydrolases/*metabolism Protein Conformation
Pubmed
Web of science
Create date
28/01/2008 10:35
Last modification date
20/08/2019 15:32
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