Synthesis, and crystal and molecular structure of the 310-helical α,β-dehydro pentapeptide Boc-Leu-Phe-Ala-ΔPhe-Leu-Ome
✍ Scribed by K. R. Rajashankar; S. Ramakumar; T. K. Mal; R. M. Jain; V. S. Chauhan
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1995
- Tongue
- English
- Weight
- 518 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0006-3525
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## Abstract The crystal and molecular structure of the pentapeptide Boc‐D‐Ala‐ΔPhe‐Gly‐ΔPhe‐D‐Ala‐OMe, containing two dehydrophenylalanine residues, was determined by x‐ray diffraction. The molecule crystallizes in the orthorombic P2~1~2~1~2~1~ space group, with __a__ = 10.439(3), __b__ = 15.319(3)
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
## 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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