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 |
|---|---|
| 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 |
| Externally published | Yes |
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Keywords
- ATP hydrolysis
- Kinesin electrostatics
- Kinesin processivity
- Kinesin substep
- Microtubule directionality
- Neck domain
- Tubulin dipole moment
ASJC Scopus subject areas
- Biophysics
Cite this
Kinesin as an electrostatic machine. / Ciudad, A.; Sancho, J. M.; Tsironis, G. P.
In: Journal of Biological Physics, Vol. 32, No. 5, 11.2006, p. 455-463.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Kinesin as an electrostatic machine
AU - Ciudad, A.
AU - Sancho, J. M.
AU - Tsironis, G. P.
PY - 2006/11
Y1 - 2006/11
N2 - 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.
AB - 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.
KW - ATP hydrolysis
KW - Kinesin electrostatics
KW - Kinesin processivity
KW - Kinesin substep
KW - Microtubule directionality
KW - Neck domain
KW - Tubulin dipole moment
UR - http://www.scopus.com/inward/record.url?scp=33846566702&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33846566702&partnerID=8YFLogxK
U2 - 10.1007/s10867-006-9028-6
DO - 10.1007/s10867-006-9028-6
M3 - Article
C2 - 19669450
AN - SCOPUS:33846566702
VL - 32
SP - 455
EP - 463
JO - Journal of Biological Physics
JF - Journal of Biological Physics
SN - 0092-0606
IS - 5
ER -