Kinesin as an electrostatic machine

A. Ciudad, J. M. Sancho, G. P. Tsironis

Research output: Contribution to journalArticlepeer-review

17 Citations (Scopus)

Abstract

Kinesin 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 cycle while the static charge configuration on the microtubule 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 the microtubule.

Original languageEnglish
Pages (from-to)455-463
Number of pages9
JournalJournal of Biological Physics
Volume32
Issue number5
DOIs
Publication statusPublished - Nov 2006

Keywords

  • ATP hydrolysis
  • Kinesin electrostatics
  • Kinesin processivity
  • Kinesin substep
  • Microtubule directionality
  • Neck domain
  • Tubulin dipole moment

ASJC Scopus subject areas

  • Biophysics
  • Atomic and Molecular Physics, and Optics
  • Molecular Biology
  • Cell Biology

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