title: Theoretical formalism for kinesin motility I. Bead movement powered by single one-headed kinesins.
abstract: 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.
authors.affiliation: Mathematical Research Branch, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-2690 USA. ydchen@helix.nih.gov
authors.forename: Y d
authors.initials: Yd
authors.lastname: Chen
mesh_terms: D004548:Elasticity; D016547:Kinesins / Q000737:chemistry* / Q000502:physiology*; D007700:Kinetics; D008870:Microtubules / Q000502:physiology*; D008954:Models, Biological; D008962:Models, Theoretical; D009068:Movement; D011487:Protein Conformation
chemical_list: D016547:Kinesins