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Schellman Motif in Dehydrooligopeptides: Crystal and Molecular Structure of Boc-Val-ΔPhe-Leu-Phe-Ala-ΔPhe-Leu-OMe

✍ Scribed by Tapas Kumar Mal; Dr. Ratan Mani Jain; Prof. Virander Singh Chauhan; Kanagalaghatta Ramabhatta Rajashankar; Prof. Suryanarayanarao Ramakumar


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
481 KB
Volume
35
Category
Article
ISSN
0044-8249

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## Abstract The structures of two dehydropentapeptides, Boc–Pro–ΔPhe–Val–ΔPhe–Ala–OMe (**I**) and Boc–Pro–ΔPhe–Gly–ΔPhe–Ala–OMe (**II**) (Boc: __t__‐butoxycarbonyl), have been determined by nuclear magnetic resonance (NMR), circular dichroism (CD), and X‐ray crystallographic studies. The peptide **

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An N a -protected model pentapeptide containing two consecutive DPhe residues, Boc-Leu-DPhe-DPhe-Ala-Phe-NHMe, has been synthesized by solution methods and fully characterized. 1 H-nmr studies provided evidence for the occurrence of a significant population of a conformer having three consecutive, i