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Crystal structure and molecular conformation of the tripeptide, N-Boc-L-Phe-Dehydro-Phe-L-Val-OCH3

✍ Scribed by T. P. Singh; M. Haridas; V. S. Chauhan; A. Kumar; D. Viterbo

Publisher
Wiley (John Wiley & Sons)
Year
1987
Tongue
English
Weight
580 KB
Volume
26
Category
Article
ISSN
0006-3525

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The peptide N-Boc-L-Phe-dehydro-Leu-L-Val-OCH3 was synthesized by the usual workup procedure and finally by coupling the N-Boc-L-Phe-dehydro-Leu-OH to valine methyl ester. It was crystallized from its solution in methanol-water mi5ture a t 4°C. The crystals belong to the triclinic space group P1 wit

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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

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✍ P. Narula; B. Khandelwal; T. P. Singh 📂 Article 📅 1991 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 422 KB 👁 2 views

## Abstract The peptide N‐Ac‐dehydro‐Phe‐L‐Val‐L‐Val‐OCH~3~ (C~22~H~31~N~3~O~5~) was synthesized by the usual workup procedure and finally by coupling the N‐Ac‐dehydro‐Phe‐L‐Val‐OH to valine methyl ester. It was crystallized from its solution in acetonitrile‐water mixture at 4°C. The crystals belon

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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