Cooperativity of multiple kinesin-1 motors mechanically coupled through a shared load

Recent experiments using single-molecule techniques have characterized the mechanical properties of single kinesin molecules in vitro at a range of loads and ATP concentrations. These experiments have shown that kinesin moves processively along microtubules by alternately advancing each of its motor...

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Bibliographic Details
Published in:Physica. D 2009-04, Vol.238 (6), p.677-686
Main Authors: Hendricks, Adam G., Epureanu, Bogdan I., Meyhöfer, Edgar
Format: Article
Language:English
Subjects:
ATP
Computer simulation
Dynamical systems
Exact sciences and technology
Kinesin
Mathematical models
Motors
Nonlinear dynamics
Physics
Single-molecule biophysics
Synchronism
Synchronization
Transient dynamics
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Summary:Recent experiments using single-molecule techniques have characterized the mechanical properties of single kinesin molecules in vitro at a range of loads and ATP concentrations. These experiments have shown that kinesin moves processively along microtubules by alternately advancing each of its motor domains in a hand-over-hand fashion, using Brownian motion and the energy from ATP hydrolysis. We have extended the theoretical analysis of kinesin through a mechanistic model that is capable of describing transient and steady-state behavior. Transient dynamics are needed to describe the effect of external perturbations (e.g. interactions with other kinesin molecules). Quantitative metrics are tailored to characterize the synchronization of nonlinear, nonsmooth systems such as kinesin. These metrics are employed to analyze the simulation results and to quantify the effect of the cargo linker stiffness, the load, and the difference in intrinsic velocity on the synchronization of two coupled motor proteins. Herein, the mechanistic model and the new analysis techniques are demonstrated for the case of two coupled kinesin motors.
ISSN:0167-2789
1872-8022
DOI:10.1016/j.physd.2009.01.005