ABSTRACT
Collective effects of the structure disorder of the protein molecules, containing inhomogeneous distribution of masses for the amino acids and fluctuations of the spring constant, of dipole-dipole interaction constant and of exciton-phonon coupling constant and diagonal disorder, resulting from nonuniformities and aperriodicities, on the soliton in the improved model have been numerically simulated. The results obtained shows that the structure disorders can change the states of the solitons, but the soliton is quite robust against these disorder effects, it is only dispersed or disrupted at larger structure disorders. According to properties of structure of normal proteins we can conclude from these results that the soliton in the improved model is stable, it is possibly a carrier of bio-energy transport in the protein molecules.
