THE INFLUENCES OF TEMPERATURE AND CHAIN—CHAININTERACTION ON FEATURES OF SOLITONSEXCITED IN a-HELIX PROTEINMOLECULES WITH THREE CHANNELS

摘要

The dynamic features of soliton transporting the bio-energy in the a-helix proteinmolecules with three channels under influences of temperature of systems and chain–chain interaction among these channels have been numerically studied by using thedynamic equations in a new model and the fourth-order Runge–Kutta method. This re-sult obtained shows that the chain–chain interaction depresses the stability of the solitondue to the dispersed effect, but the stability of the soliton in the case of simultaneousmotivation of three channels by an initial conditions is better than that in another ini-tial condition. We also find from this investigation that the new soliton can transportsteadily over 1000 amino acid residues in the cases of motion of long time of 120 ps, andretain their shapes and energies to travel towards the protein molecules after mutualcollision of the solitons at the biological temperatures of 300 K. Therefore the soliton isvery robust against the thermal perturbation of the a-helix protein molecules at 300 K.From the investigation of changes of features of the soliton with increasing temperature,we find that the amplitudes and velocities of the solitons decrease with increasing tem-perature of proteins, but the soliton disperses in the cases of higher temperature of 325 Kand larger structure disorders. Thus we find that the critical temperature of the solitonoccurring in the a-helix protein molecules is about 320 K. Therefore we can concludethat the soliton in the new model can play an important role in the bio-energy transportin the a-helix protein molecules with three channels at biological temperature, and thenew model is possibly a candidate for the mechanism of this transport.