STRUCTURAL ORGANIZATION OF RIMORPHIN AND ITS SYNTHETIC ANALOGS

The spatial structure and conformations of rimorphin were investigated using theoretical conformational analysis. The spatial organization o f the peptide can be described by a set of 11 low-energy conformations of the backbone. By solving the reverse conformational problem, a num ber of modified amino acid sequences ([Ala(2)], [Ala(3)], [MePhe(9)], [MeLys(10)], [MeVal(11)], and [MeVal(12)]-analogs of rimorphin) were d etermined that have spatial structures corresponding to the set of low -energy conformations and should, therefore, possess physiological act ivity.