SELF-ORGANIZATION OF PROTEIN CHAIN ACCELERATES UPON STABILIZATION OF ITS NATIVE CONFORMATION - NUMERICAL EXPERIMENT

Minimization of the protein chain energy was studied by the Monte-Carl o method using model for two-beta-sheet proteins. In the structures ex amined (''edited structures''), the native conformation is separated f rom other ones by an energy gap. They reach the global energy minimum most rapidly at the same temperature as random sequences. It was shown that at the optimal self-organization temperature, the native conform ation of edited structures is thermodynamically stable. This is the re ason why self-organization proceeds rapidly.