Fen Edebiyat Fakültesi / Faculty of Letters and Sciences Fizik / PhysicsGodjayev, Niftali M.Akverdieva, G.AKYÜZ, SEVİM2018-08-312018-08-311997-01-20https://doi.org/10.1016/S0022-2860(96)09410-0https://hdl.handle.net/11413/2570Conformational 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.en-USTheoretical conformational analysisAmino acid residuePeptideArticle