The kinesin walk: a dynamic model with elastically coupled heads.
Recently individual two-headed kinesin molecules have been studied in in vitro motility assays revealing a number of their peculiar transport properties. In this paper we propose a simple and robust model for the kinesin stepping process with elastically coupled Brownian heads that show all of these properties. The analytic and numerical treatment of our model results in a very good fit to the experimental data and practically has no free parameters. Changing the values of the parameters in the restricted range allowed by the related experimental estimates has almost no effect on the shape of the curves and results mainly in a variation of the zero load velocity that can be directly fitted to the measured data. In addition, the model is consistent with the measured pathway of the kinesin ATPase.
Derényi
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Department of Atomic Physics, Eötvös University, Budapest, Hungary.
Vicsek
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D000255:Adenosine Triphosphate / Q000378:metabolism; D016547:Kinesins / Q000737:chemistry / Q000378:metabolism*; D007700:Kinetics; D008870:Microtubules / Q000737:chemistry; D008956:Models, Chemical; D011485:Protein Binding; D013816:Thermodynamics
D000255:Adenosine Triphosphate; D016547:Kinesins