MODELING OF THE PHYTOCHROME STRUCTURE

Secondary structures of phytochromes from five plant species have been calculated by the method based on the theory of short- and long-range interactions in proteins. It has been shown that the predicted conten t of the elements of secondary structure in different phytochrome mole cules varies at standart conditions for alpha-helix (33-38%), beta-she et (15-23%), beta-turn (14-16%), and random coil (24-33%). A model for the fragment of the oat phytochrome consisting of amino-acid residues from 205 to 350 has been proposed.