On the low energy solution conformation of somatostatin
β Scribed by Byron H. Arison; Ralph Hirschmann; William J. Paleveda; Stephen F. Brady; Daniel F. Veber
- Book ID
- 118316080
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 306 KB
- Volume
- 100
- Category
- Article
- ISSN
- 0006-291X
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π SIMILAR VOLUMES
Fourier transform infrared spectroscopy was applied to the conformational analysis of somatostatin in H,O, 'H,O, dimethyl sulphoxide (DMSO)-'H,O and DMSO. The results suggest that in these solvents the peptide adopts a similar structure. In agreement with circular dichroism (CD) spectroscopic data,
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
dominant conformation of the linear active analogue is shown to be the same as that of the active cyclic analogue; they both adopt a PI,' turn/bsbeet structure. The linear analogue with low activity has a similar conformation, which, however, is less stable.
## Abstract Results from __ab initio__ selfβconsistent field (SCF) calculations with a 3β21G and a doubleβzetaβplus polarization (DZP) basis set on four lowβenergy conformations of cyclohexaglycine are reported. In agreement with results from semiempirical and molecular mechanics force field calcul