Volume 97, Number 4, February 2012
|Number of page(s)||6|
|Published online||20 February 2012|
Recovery of state-specific potential of molecular motor from single-molecule trajectory
Faculty of Science and Engineering, Chuo University - Tokyo 112-8551, Japan
2 Faculty of Physics, Ludwig-Maximilians-Universität München - München 80339, Germany, EU
Accepted: 17 January 2012
We have developed a novel method to evaluate the potential profile of a molecular motor at each chemical state from only the probe's trajectory and applied it to a rotary molecular motor F1-ATPase. By using this method, we could also obtain the information regarding the mechanochemical coupling and energetics. We demonstrate that the position-dependent transition of the chemical states is the key feature for the highly efficient free-energy transduction by F1-ATPase.
PACS: 05.70.Ln – Nonequilibrium and irreversible thermodynamics / 05.40.Jc – Brownian motion / 87.16.Nn – Motor proteins (myosin, kinesin dynein)
© EPLA, 2012
Current usage metrics show cumulative count of Article Views (full-text article views including HTML views, PDF and ePub downloads, according to the available data) and Abstracts Views on Vision4Press platform.
Data correspond to usage on the plateform after 2015. The current usage metrics is available 48-96 hours after online publication and is updated daily on week days.
Initial download of the metrics may take a while.