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Direct observation of the rotation of F1-ATPase
TLDR
It is shown that a single molecule of F1-ATPase acts as a rotary motor, the smallest known, by direct observation of its motion by attaching a fluorescent actin filament to the γ-subunit as a marker, which enabled us to observe this motion directly.
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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase
TLDR
It is shown by high-speed imaging that the 120° step consists of roughly 90° and 30° substeps, each taking only a fraction of a millisecond, which supports the binding-change model for ATP synthesis by reverse rotation of F1-ATPase.
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Time courses of cell electroporation as revealed by submicrosecond imaging of transmembrane potential.
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Coupling of Rotation and Catalysis in F1-ATPase Revealed by Single-Molecule Imaging and Manipulation
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Membrane conductance of an electroporated cell analyzed by submicrosecond imaging of transmembrane potential.
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F1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120° Steps
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Voltage-induced pore formation and hemolysis of human erythrocytes.
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A theory of fluorescence polarization decay in membranes.
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Catalysis and rotation of F1 motor: Cleavage of ATP at the catalytic site occurs in 1 ms before 40° substep rotation
TLDR
Results of ATPγS hydrolysis by the mutant F1 ensure that cleavage of ATP most likely corresponds to one of the two 1-ms events and not some other faster undetected event, and this interim dwell catalytic dwell is called.
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Direct measurement of the torsional rigidity of single actin filaments.
TLDR
This paper shows that the torsional rigidity can be measured directly by visualizing the tORSional Brownian motion of a single actin filament with a novel methodology based on an optical trapping technique that is one to two orders of magnitude greater than previous experimental estimates.
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