The results of a conformational study by nuclear magnetic spectroscopy and computational methods on a series of point-mutated synthetic peptides, containing 14 amino acid residues and mimicking the region containing the Arg-Lys dibasic cleavage site of pro-somatostatin, have confirmed the possible r
Conformation of two somatostatin analogues in aqueous solution : Study by NMR methods and circular dichroism
โ Scribed by Chantal WYNANTS; Dirk TOURWE; Wieslaw KAZMIERSKI; Victor J. HRUBY; Georges VAN BINST
- Book ID
- 115126537
- Publisher
- John Wiley and Sons
- Year
- 1989
- Tongue
- English
- Weight
- 784 KB
- Volume
- 185
- Category
- Article
- ISSN
- 1432-1327
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## Abstract Conformational studies of nociceptin (NCโNH~2~), its fully active fragment, NC(1โ13)โNH~2~, and two significantly less potent fragments, NC(1โ13)โOH and NC(1โ11)โOH, were conducted in water and TFE solutions by the employment of circular dichroism, and in DMSOโd~6~ by 2D NMR spectroscop