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We propose a biochemical model providing the kinetic and energeticdescriptions of the processivity dynamics of kinesin and dinein molecularmotors. Our approach is a modified version of a well known model describingkinesin dynamics and considers the presence of a competitive inhibitionreaction by ADP. We first reconstruct a continuous free-energy landscape of thecycle catalyst process that allows us to calculate the number of steps given bya single molecular motor. Then, we calculate an analytical expressionassociated to the translational velocity and the stopping time of the molecularmotor in terms of time and ATP concentration. An energetic interpretation ofmotor processivity is discussed in quantitative form by using experimentaldata. We also predict a time duration of collective processes that agrees withexperimental reports.

Reconstructing the free-energy landscape associated to molecular motors processivity