Publication:
A Molecular Mechanics Conformational Study of Peptide T

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Date
1997-01-20
Authors
Godjayev, Niftali M.
Akyüz, Sevim
Akverdieva, G.
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Publisher
Elsevier
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Abstract

Conformational behaviour of peptide T, a competitor of the human immuno-deficiency virus in the binding to human T cells, was investigated by theoretical conformational analysis. Two types of conformations are found to be the most stable: quasi cyclic conformation, which is favourable for intensive electrostatic interaction between the charged terminal groups, and spiral conformation, which provides optimal nonvalent interaction of atoms of the polypeptide skeleton. A β-turn of the polypeptide chain was revealed on the section Thr4-Tyr7.

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Keywords
Theoretical conformational analysis , Amino acid residue , Peptide
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