Search Swinburne Research Bank
Please use this identifier to cite or link to this item: http://hdl.handle.net/1959.3/46536
|Download PDF (Published version) (Adobe Acrobat PDF, 337 KB)|
- Kinetics and chemomechanical properties of the F[sub 1]-ATPase molecular motor
- Liu, Ming S.; Todd, B. D.; Sadus, Richard J.
- F1-ATPase hydrolyzes ATP into ADP and Pi and converts chemical energy into mechanical rotation with exceptionally high efficiency. This energy-transducing molecular motor increasingly attracts interest for its unique cellular functions and promising application in nanobiotechnology. To better understand the chemomechanics of rotation and loading dynamics of F1-ATPase, we propose a computational model based on enzyme kinetics and Langevin dynamics. We show that the torsional energy and stepwise rotation can be regulated by a series of near-equilibrium reactions when nucleotides bind or unbind, as well as characterized by an effective 'ratchet' drag coefficient and a fitting chemomechanic coefficient. For the case of driving an actin filament, the theoretical load-rotation profile is analyzed and comparison with experimental data indicates reasonable agreement. The chemomechanics described in this work is of fundamental importance to all ATP-fueled motor proteins.
- Publication type
- Journal article
- Research centre
- Swinburne University of Technology. Centre for Molecular Simulation
- Journal of Chemical Physics, Vol. 118, no. 21 (2003), pp. 9890-9898
- Publication year
- Biomechanics; Direct energy conversion; Molecular biophysics; Nanotechnology; Proteins; Transducers
- American Institute of Physics
- Publisher URL
- Copyright © 2003 American Institute of Physics. Published version of this paper reproduced here in accordance with the copyright policy of the publisher.
- Full text
- Peer reviewed