Intermolecular forces between the motor protein and the filament.
Intermolecular forces between motor proteins and filaments were evaluated on the basis of the experimental data of an in vitro motility assay by considering the molecular friction in the movement system. The molecular friction was caused by a different mechanism from that of the hydrodynamic drag. However, the molecular frictional forces apparently gave the same expression as the hydrodynamic frictional forces. The resulting equation was very effective in examining the physical properties of the weak interaction in the dynein-microtubules system from basic experiments carried out by Vale et al. (1989). From careful analysis of their experimental data, it was concluded that the hydrodynamic friction was not dominant, even in the weak binding state. The electrostatic interaction between dynein-heads and microtubules in the weak binding state was analyzed by applying the DLVO (Derjaguin-Landau-Verway-Overbeek) theory in colloid science through the ionic dependence of one-dimensional diffusion. The interacting distance between charges which took part in the weak adhesion was estimated to be 3 nm. In the present study, the molecular mechanism of the sliding velocity was also investigated for the myosin-actin filaments and the kinesin-microtubules systems by fitting the ATP-dependence and the ionic dependence in ATP-driven active sliding.
Suda
H
H
Department of Biological Science and Technology, School of High-Technology for Human Welfare, Tokai University, Shizuoka, Japan.
Taylor
T W
TW
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D004058:Diffusion; D007477:Ions; D008870:Microtubules / Q000378:metabolism*; D013816:Thermodynamics
D007477:Ions; D000255:Adenosine Triphosphate