Thermal stability of the new soliton transported bio-energy under influence of fluctuations of characteristic parameters at biological temperature in the protein molecules

The dynamic behaviors of the new soliton in the improved Davydov model in the protein molecules at biological temperature have been numerically simulated by utilizing the dynamic equations for the bio-energy transport and the Runge-Kutta way. in this simulation the influences of the temperature and structure disorders of the protein molecules on the soliton transporting the bio-energy have been completely considered. We find that the new soliton is quite stable in die cases of motion of a long time of 300 ps and of disorders of the structures of the proteins at; biological temperatures of 300 K-320 K. The disorders of the structures contain the disorder of mass sequence of amino acids and the fluctuations of the coupling constant, force constant and dipole- dipole interaction constant and ground state energy of the proteins, designating the features of its structure and interactions between the particles in it. However, the soliton disperses in the cases of higher temperature of 325 K and larger structure disorders. The numerical results show that, the new soliton is very robust against; the influences of the thermal perturbation kind structure disorders at biological temperature 300 K, its lifetime and critical temperature are at least 300 ps at 300 K and 320 K, respectively. These results are also consistent with analytical data.