A molecular mechanics conformational study of peptide T


Godjayev N., Akyuz S., Akverdieva G.

JOURNAL OF MOLECULAR STRUCTURE, vol.403, pp.95-110, 1997 (Journal Indexed in SCI) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 403
  • Publication Date: 1997
  • Doi Number: 10.1016/s0022-2860(96)09410-0
  • Title of Journal : JOURNAL OF MOLECULAR STRUCTURE
  • Page Numbers: pp.95-110

Abstract

Conformational behaviour of peptide T, a competitor of the human immune-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 P-turn of the polypeptide chain was revealed on the section Thr(4)-Tyr(7).