A MOLECULAR MECHANICS CONFORMATIONAL STUDY OF PEPTIDE-T

Conformational behaviour of peptide T, a competitor of the human immun e-deficiency virus in the binding to human T cells, was investigated b y theoretical conformational analysis. Two types of conformations are found to be the most stable: quasi cyclic conformation, which is favou rable for intensive electrostatic interaction between the charged term inal groups, and spiral conformation, which provides optimal nonvalent interaction of atoms of the polypeptide skeleton. A P-turn of the pol ypeptide chain was revealed on the section Thr(4)-Tyr(7).