A molecular mechanics conformational study of peptide T

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)