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Evidence for beta-turn structure in model peptides reproducing pro-ocytocin/neurophysin proteolytic processing site.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1990 May 16; Vol. 168 (3), pp. 1066-73. - Publication Year :
- 1990
-
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.
- Subjects :
- Amino Acid Sequence
Circular Dichroism
Magnetic Resonance Spectroscopy
Models, Chemical
Molecular Sequence Data
Oligopeptides metabolism
Oxytocin metabolism
Protein Conformation
Neurophysins metabolism
Oligopeptides chemical synthesis
Oxytocin analogs & derivatives
Peptide Hydrolases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 168
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 2132568
- Full Text :
- https://doi.org/10.1016/0006-291x(90)91138-i