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Updated: Aug 17, 2025

Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
Published on: January 22, 2019
Optimal Control of the F1-ATPase Molecular Motor
Deepak Gupta1,2, Steven J Large1, Shoichi Toyabe3
1Department of Physics, Simon Fraser University, BurnabyV5A 1S6, British Columbia, Canada.
Abstract:
F1-ATPase is a rotary molecular motor that in vivo is subject to strong nonequilibrium driving forces. There is great interest in understanding the operational principles governing its high efficiency of free-energy transduction. Here we use a near-equilibrium framework to design a nontrivial control protocol to minimize dissipation in rotating F1 to synthesize adenosine triphosphate. We find that the designed protocol requires much less work than a naive (constant-velocity) protocol across a wide range of protocol durations. Our analysis points to a possible mechanism for energetically efficient driving of F1 in vivo and provides insight into free-energy transduction for a broader class of biomolecular and synthetic machines.
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