Conformational dynamics of peptide T molecule


Akverdieva G., Godjayev N., Akyuz S.

JOURNAL OF MOLECULAR STRUCTURE, cilt.609, ss.115-128, 2002 (SCI-Expanded) identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 609
  • Basım Tarihi: 2002
  • Doi Numarası: 10.1016/s0022-2860(01)00974-7
  • Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.115-128
  • İstanbul Üniversitesi Adresli: Hayır

Özet

Using a method of the theoretical conformational analysis, a conformational dynamics of the side chains of the amino acid residues of peptide T, a competitor of the human immuno-deficiency virus in the binding to human T cells, was investigated. For this purpose, the conformational maps of the potential surfaces were constructed over the angles of the side chains for the preferable conformations of peptide T molecule. Permissible deviations of these angles from the optimal values were determined. It has been found that the angles of the side chains of the amino acid residues involved in physiologically active fragment Thr4-Thr8 are more rigid than in the other segment of the molecule. This fact confirms the existence of such a regular structure as beta-turn revealed previously in studies of the spatial structure of the peptide T molecule. (C) 2002 Elsevier Science B.V. All rights reserved.