材料期刊网

We studied numerically the influences of damping and temperature of medium on the properties of the soliton transported bio-energy in the alpha-helix protein molecules with three channels by using the dynamic equations in the improved Davydov theory and fourth-order Runge-Kutta method. speed, in which the shape and energy of the soliton can remain in the cases of motion, whether short-time at T=0 or long time at T=300 K. In these motions, the solition can travel over about 700 amino acid residues, thus its lifetime is, at least, 120 ps at 300 K. When the two solitons undergo a collision, they can also retain themselves forms to transport towards. These results are consistent with the analytic result obtained by quantum perturbed theory in this model. However, the amplitudes of the solitons depress along with increase of temperature of the medium, and it begins to didperse at 320 K. In the meanwhile, the damping of the medium can influence the states and properties of the soliton excited in alpha-helix protein molecules. The soliton is dispersed at the large damping coefficient Gamma = 4 Gamma(0) at 300 K. The results show that the soliton excited in the alpha-helix protein molecules with three channels is very robust against the damping and thermal perturbation of medium at biological temperature of 300 K. Thus we can conclude that the soliton can play importeant part in the bio-energy transport and the improved model is possibly a candidate for the mechanism of the energy of the transport in the alpha-helix proteins.