Rectified Brownian motion and kinesin motion along microtubules

The mechanism of rectified Brownian movement is used to analyze measured data for kinesin motion along microtubules. A key component of the mechanism is the diffusive movement of the microtubule binding heads of kinesin during the adenosine triphosphate (ATP) cycle. The first-passage time distributi...

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Bibliographic Details
Published in:Physical review. E, Statistical, nonlinear, and soft matter physics Statistical, nonlinear, and soft matter physics, 2001-05, Vol.63 (5 Pt 1), p.051901-051901
Main Authors: Fox, R F, Choi, M H
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - chemistry
Adenosine Triphosphate - chemistry
Animals
Binding Sites
Biophysics - methods
Hydrolysis
Kinesin - chemistry
Microtubules - metabolism
Models, Biological
Models, Chemical
Models, Statistical
Protein Structure, Secondary
Time Factors
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Summary:The mechanism of rectified Brownian movement is used to analyze measured data for kinesin motion along microtubules. A key component of the mechanism is the diffusive movement of the microtubule binding heads of kinesin during the adenosine triphosphate (ATP) cycle. The first-passage time distribution for this step is analyzed in detail and is shown to be responsible for observed load-velocity profiles. The ATPase activity of the kinesin heads is that of a nucleotide switch and not that of a direct chemomechanical energy converter. Experimental data acquisition, rate constants, and alternative explanations are discussed. The mechanism described in this paper is fundamental to the nanobiology of intracellular processes.
ISSN:1539-3755
DOI:10.1103/PhysRevE.63.051901