材料期刊网

Combination effects of structure disorder of protein molecules containing the fluctuations of spring constant, dipole-dipole interaction constant and exciton-phonon coupling constant and diagonal disorder, resulting from nonuniform distribution of masses of amino acid residues and impurities, on the soliton transported the bio-energy in the proteins have been numerically simulated by fourth-order Runge-Kutta method in the improved model. The results obtained show that these structure disorders can change the states of solitons but as the sollitons are quite robust against thesse disorder effects, they can only be dispersed or disrupted in the cases of quite large structure disorders. From these results and the properties of molecular structure of biological proteins we can conclude that the new soliton in the improved model is quite stable in normal conditions. Thus the soliton is possibly a carrier of bio-energy trasport in the protein molicules.