Conformational properties of somatostatin. VI. In a methanol solution
- 1 October 1986
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 25 (10) , 1895-1908
- https://doi.org/10.1002/bip.360251007
Abstract
The peptide hormone, somatostatin, has been studied by nmr at 500 MHz in a methanol solution and at low temperature (263 K) in order to investigate a possible similarity with conformationally restricted biologically active analogs. The more pronounced predominancy of one conformer already present in a water solution is demonstrated. No evidence has been shown for interactions between Phe11 and other Phes in the molecule.Keywords
This publication has 5 references indexed in Scilit:
- The conformational properties of somatostatin V. Side-chain interaction in aqueous solution as studied by one-dimensional and two-dimensional NMR methodsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Assignment and analysis of the 500 MHz1H NMR spectra of somatostatin and the acyclic precursor (S3,14-Acm)-somatostatin in dimethyl sulphoxideMagnetic Resonance in Chemistry, 1982
- The conformational properties of somatostatin IV. The conformers contributing to the conformational equilibrium of somatostatin in aqueous solution as found by semi-empirical energy calculations and high-resolution NMR experimentsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- On the low energy solution conformation of somatostatinBiochemical and Biophysical Research Communications, 1981
- The conformational properties of the peptide hormone somatostatin (III)FEBS Letters, 1980