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.
Conformational properties of somatostatin. VI. In a methanol solution
โ Scribed by E. M. M. van den Berg; A. W. H. Jans; G. van Binst
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1986
- Tongue
- English
- Weight
- 481 KB
- Volume
- 25
- Category
- Article
- ISSN
- 0006-3525
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โฆ Synopsis
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 Phe" and other Phes in the molecule.
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