Kinesin as an electrostatic machine

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dc.creatorCiudad, A.
dc.creatorSancho, J. M.
dc.creatorTsironis, G. P.
dc.date2006-10-24
dc.date.accessioned2026-07-07T07:38:53Z
dc.date.available2026-07-07T07:38:53Z
dc.descriptionKinesin and related motor proteins utilize ATP fuel to propel themselves along the external surface of microtubules in a processive and directional fashion. We show that the observed step-like motion is possible through time varying charge distributions furnished by the ATP hydrolysis circle while the static charge configuration on the microtuble provides the guide for motion. Thus, while the chemical hydrolysis energy induces appropriate local conformational changes, the motor translational energy is fundamentally electrostatic. Numerical simulations of the mechanical equations of motion show that processivity and directionality are direct consequences of the ATP-dependent electrostatic interaction between the different charge distributions of kinesin and microtubule.
dc.description6 pages, 3 figures. To appear in the Journal of Biological Physics
dc.identifierhttps://arxiv.org/abs/q-bio/0610045
dc.identifierhttp://arxiv.org/abs/q-bio/0610045
dc.identifierdoi:10.1007/s10867-006-9028-6
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/121254
dc.subjectBiomolecules
dc.subjectStatistical Mechanics
dc.subjectBiological Physics
dc.titleKinesin as an electrostatic machine
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