States and properties of the soliton transported bio-energy in nonuniform protein molecules at physiological temperature

We have numerically studied states and properties of the soliton transported bio-energy at physiological temperature 300 K by the Runge-Kutta way and dynamic equations in the improved Davydov theory. We proved that the new solitons can move without dispersion retaining its shape and energy in both uniform and nonuniform protein molecules. If considering further effect of thermal perturbation of heat bath on the soliton in the nonuniform proteins, it is still thermally stable at the biological temperature 300 K and in the longer times of 300 ps and larger spacings of 400 amino acids, which is consistent with the analytic result obtained by a quantum perturbed theory. These results exhibit that the new soliton is a possible carrier of the bio-energy transport and the improved model is possibly a candidate for the mechanism of this transport.