A molecular mechanics conformational study of peptide T
JOURNAL OF MOLECULAR STRUCTURE, cilt.403, sa.1-2, ss.95-110, 1997 (SCI-Expanded, Scopus)
- Yayın Türü: Makale / Tam Makale
- Cilt numarası: 403 Sayı: 1-2
- Basım Tarihi: 1997
- Doi Numarası: 10.1016/s0022-2860(96)09410-0
- Dergi Adı: JOURNAL OF MOLECULAR STRUCTURE
- Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
- Sayfa Sayıları: ss.95-110
- İstanbul Kültür Üniversitesi Adresli: Hayır
Özet
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).