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pubmed:abstractText |
We analysed published force-velocity data for kinesin using classical Michaelis-Menten kinetic theory and found that the effect of force on the stepping rate of kinesin is analogous to the effect of a mixed inhibitor in classical inhibition theory. We derived an analytical expression for the velocity of kinesin (the stepping rate, equal to the ATP turnover rate) as a function of ATP concentration and force, and showed that it accurately predicts the observed single molecule stepping rate of kinesin under a variety of conditions.
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pubmed:affiliation |
Departament d'Estructura i Constituents de la Matèria, Facultat de Física, Universitat de Barcelona, Diagonal 647, 08028, Barcelona, Spain.
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