Using
First Observation of Left-Handed Helical Conformation in a Dehydro Peptide Containing Two l -Val Residues. Crystal and Solution Structure of Boc- l -Val-ΔPhe-ΔPhe-ΔPhe- l -Val-OMe †,⊥
✍ Scribed by Jain, R. M.; Rajashankar, K. R.; Ramakumar, S.; Chauhan, V. S.
- Book ID
- 126082548
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 238 KB
- Volume
- 119
- Category
- Article
- ISSN
- 0002-7863
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The peptide BOC-L-Val-APhe-APhe-L-Val-OCH3 was synthesized by the azlactone method in solution phase, and its crystal and molecular structures were determined by x-ray diffraction method. Single crystals were grown by slow evaporation from a methanol/water solution at 6°C. The crystals belong to an
Highly specific peptide structures can be designed by inserting dehydro residues into peptide sequences. The peptide N-Boc-L-Phe-dehydro-Phe-L-Val-L-Phe-dehydro-Phe-~-V~-OCH~, synthesized by conventional procedures, crystallizes from methanol-water mixtures at 4°C in the tetragonal space group P43 w
To obtain general rules of peptide design using alpha, beta-dehydro-residues, a sequence with two consecutive delta Phe-residues, Boc-L-Val-delta Phe-delta Phe-L-Ala-OCH3, was synthesized by azlactone method in solution phase. The peptide was crystallized form its solution in an acetone/water mixtur
## 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 **