MOTIFS AS ELEMENTS IN PROTEIN STRUCTURE AND FUNCTION: A PROPOSAL

Abstract

In this article we propase that protein motifs behave as single charged entities precisely located in a water space in such a fashion that for a whole protein - solvating water system, there is a maximum of attractions and a mínimum of repulsions between the motifs making up the protein. Any region of the surface of a protein made up of hydrophylic portions cif different motifs generates an uneven electromagnetic field which fixes water molecules to it. A substrate is a molecule that generates a complementary field to the active region of the protein. Protein - substrate interaction can be thought of as two electromagnetic fields neutralizing each other upon reaction to rnake a new system with a larger internal energy than either that of the protein or that of the substrate. In order to find a new minimum interna! energy and therefore a stable system, there must be a conformational change which simply meaos that the motifs will rearrange in such a way that a new condition of maximum attractions and rninimum repulsions is obtained. It is this conformational change that causes known protein actions.