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Biophys J, January 2000, p. 313-321, Vol. 78, No. 1
Mathematical Research Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-2690 USA
The directional movement on a microtubule of a plastic
bead connected elastically to a single one-headed kinesin motor is studied theoretically. The kinesin motor can bind and unbind to periodic binding sites on the microtubule and undergo conformational changes while catalyzing the hydrolysis of ATP. An analytic formalism relating the dynamics of the bead and the ATP hydrolysis cycle of the
motor is derived so that the calculation of the average velocity of the
bead can be easily carried out. The formalism was applied to a simple
three-state biochemical model to investigate how the velocity of the
bead movement is affected by the external load, the diffusion
coefficient of the bead, and the stiffness of the elastic element
connecting the bead and the motor. The bead velocity was found to be
critically dependent on the diffusion coefficient of the bead and the
stiffness of the elastic element. A linear force-velocity relation was
found for the model no matter whether the bead velocity was modulated
by the diffusion coefficient of the bead or by the externally applied
load. The formalism should be useful in modeling the mechanisms of
chemimechanical coupling in kinesin motors based on in vitro motility data.
Biophys J, January 2000, p. 313-321, Vol. 78, No. 1
© 2000 by the Biophysical Society 0006-3495/00/01/313/09 $2.00
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