The relationship between the sign of the polypeptide backbone angle omega and the type of the side chain radical of amino-acid residues
- Authors: Torshin I.Y.1, Batyanovskii A.V.2, Uroshlev L.A.3, Esipova N.G.3, Tumanyan V.G.3
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Affiliations:
- Department of Chemistry
- Institute of Biophysics and Cell Engineering
- Engelhardt Institute of Molecular Biology
- Issue: Vol 62, No 3 (2017)
- Pages: 342-347
- Section: Molecular Biophysics
- URL: https://ogarev-online.ru/0006-3509/article/view/152292
- DOI: https://doi.org/10.1134/S0006350917030216
- ID: 152292
Cite item
Abstract
The dihedral angle ω, which reflects the nonplanarity of the peptide group, was found to be essential for describing the conformation of the polypeptide chain backbone in the context of particular side chain radicals of amino-acid residues. Conformational clusters corresponding to conformationally stable peptides identified previously were observed.
About the authors
I. Yu. Torshin
Department of Chemistry
Email: tuman@eimb.ru
Russian Federation, Moscow, 119991
A. V. Batyanovskii
Institute of Biophysics and Cell Engineering
Email: tuman@eimb.ru
Belarus, Akademicheskaya ul. 27, Minsk, 220072
L. A. Uroshlev
Engelhardt Institute of Molecular Biology
Email: tuman@eimb.ru
Russian Federation, ul. Vavilova 32, Moscow, 119991
N. G. Esipova
Engelhardt Institute of Molecular Biology
Email: tuman@eimb.ru
Russian Federation, ul. Vavilova 32, Moscow, 119991
V. G. Tumanyan
Engelhardt Institute of Molecular Biology
Author for correspondence.
Email: tuman@eimb.ru
Russian Federation, ul. Vavilova 32, Moscow, 119991
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