Design of Peptides With, α,β-Dehydro-Residues: A Dipeptide With a Branched β-Carbon Dehydro-Residue at the (i+1) Position, Methyl N-(benzyloxycarbonyl)-α,β-Didehydrovalyl-L-Tryptophanate

Authors

Vijayaraghavan Rangachari, University of Southern MississippiFollow
Pravindra Kumar, All India Institute of Medical SciencesFollow
Sharmistha Dey, All India Institute of Medical Sciences
Tej P. Singh, All India Institute of Medical SciencesFollow

Document Type

Article

Publication Date

2001

Department

Chemistry and Biochemistry

Abstract

The structure of the title peptide, C₂₅H₂₇N₃O₅, has been determined and its conformation analysed. Values of the standard peptide torsion angles are φ(1) = -44.2 (3)°, ψ(1) = 135.9 (2)°, φ(2) = -141.6 (2)° and ψ(T/2) = 168.0 (2)°. The crystal structure is stabilized by an intermolecular hydrogen bond, with an N···O distance of 2.919 (3)Å, which is formed between screw-axis-related NH and CO groups of dehydrovaline residues.

Comments

Publisher Version

Publication Title

Acta Crystallographica Section C: Crystal Structure Communications

Volume

57

Issue

10

First Page

1220

Last Page

1221

Recommended Citation

Rangachari, V., Kumar, P., Dey, S., Singh, T. P. (2001). Design of Peptides With, α,β-Dehydro-Residues: A Dipeptide With a Branched β-Carbon Dehydro-Residue at the (i+1) Position, Methyl N-(benzyloxycarbonyl)-α,β-Didehydrovalyl-L-Tryptophanate. Acta Crystallographica Section C: Crystal Structure Communications, 57(10), 1220-1221.
Available at: https://aquila.usm.edu/fac_pubs/7546