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- W2062865981 abstract "Significance We present a description of the angular velocity of the power stroke as a function of rotational position for the F 1 -ATPase molecular motor. The angular velocity of this motor, which rotates in 120° power strokes separated by catalytic dwells, is part of the F o F 1 ATP synthase in oxidative phosphorylation, and has been thought not to vary. This paper reports the unexpected discovery that a series of angular accelerations and decelerations occur, providing direct evidence that angular velocity depends on substrate binding affinity. The data support a model in which rotation is powered by Van der Waals repulsive forces during the final 85° of rotation, consistent with a transition from F 1 structures 2HLD1 and 1H8E (Protein Data Bank)." @default.
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- W2062865981 date "2014-02-24" @default.
- W2062865981 modified "2023-10-16" @default.
- W2062865981 title "Anatomy of F <sub>1</sub> -ATPase powered rotation" @default.
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- W2062865981 doi "https://doi.org/10.1073/pnas.1317784111" @default.
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