A model of processive movement of dimeric kinesin.

Dimeric kinesin can move processively on microtubule filaments by hydrolyzing ATP. Diverse aspects of its movement dynamics have been studied extensively by using various experimental methods. However, the detailed molecular mechanism of the processive movement is still undetermined and a model that can provide a consistent and quantitative explanation of the diverse experimental data is still lacking. Here, we present such a model, with which we study the movement dynamics of the dimer under variations of solution viscosity, external load, ATP concentration, neck linker length, effect of neck linker docking, effect of a large-size particle attached to one kinesin head, etc., providing consistent and quantitative explanations of the available diverse experimental data. Moreover, predicted results are also provided.