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The effects of structure nonuniformity and thermal perturbation on properties of proton conductivity in hydrogen-bonded systems with damping exposed in an externally applied electric-field have been numerically studied by fourth order Runge-Kutta method in our soliton model. The results obtained show that the proton-soliton is very robust against the structure disorder including the fluctuation of the force constant and disorder in the sequence of masses and thermal perturbation and damping effect of medium, its velocity of conductivity increases with increasing externally applied electric-field and with decreasing damping coefficient of medium, but the proton-soliton disperses at quite great fluctuations of force constant and damping coefficient. In the meantime, the proton-soliton in ice crystals is thermally stable in the region of temperature of T ≤ 273 K. From the numerical simulation, we find out that the mobility (or velocity) of proton conduction in ice is a nonmonotonic function of temperature in the temperature region of 170-273 K, i.e., it increases initially, reaches a maximum at about 191.4 K, subsequently decreases to a minimum at about 211.6 K, and then increases again. This changed rule of mobility obtained consists qualitatively with its experimental datum in ice in the same temperature region. Thus these results provide an evidence for the soliton excited in the hydrogen-bonded systems. [ABSTRACT FROM AUTHOR]

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 solitons are quite robust against these 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 transport in the protein molecules. [ABSTRACT FROM AUTHOR]