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 language | English |
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Pages (from-to) | 455-463 |
Number of pages | 9 |
Journal | Journal of Biological Physics |
Volume | 32 |
Issue number | 5 |
DOIs | |
Publication status | Published - 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