The relationship between the sign of the polypeptide backbone angle omega and the type of the side chain radical of amino-acid residues


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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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