Oxford Molecular Motors

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Response of the Bacterial Flagellar Motor to Controlled Temperature Change

BIOPHYSICAL JOURNAL 98:3 (2010) 159A-159A

Authors:

Matthew A Baker, Yuichi Inoue, Chien-Jung Lo, Akihiko Ishijima, Richard Berry

Single Molecule Rotation of F1-ATPase from S. cerevisiae

BIOPHYSICAL JOURNAL 98:3 (2010) 433A-434A

Authors:

Bradley C Steel, Yamin Wang, Vijay Pagadala, Richard M Berry, David M Mueller

Single Molecule Studies of E-ColiF1Fo ATP Synthase in Lipid Bilayers

BIOPHYSICAL JOURNAL 98:3 (2010) 54A-54A

Authors:

Wei M Ho, Richard M Berry

An introduction to the physics of the bacterial flagellar motor: A nanoscale rotary electric motor

Contemporary Physics 50:6 (2009) 617-632

Authors:

MAB Baker, RM Berry

Abstract:

Biological molecular motors show us how directed motion can be generated by nanometre-scale devices that work at the energy scale of the thermal bath. Direct and indirect observations of functioning single molecule motors allow us to see fundamental processes of statistical physics unfolding in microscopic detail at room temperature, something that was unimaginable only a few decades ago. In this review, we introduce molecular motors and the physics relevant to their mechanisms before focusing on our recent experiments on the bacterial flagellar motor, the rotary device responsible for bacterial locomotion.

Single molecule measurements of F1-ATPase reveal an interdependence between the power stroke and the dwell duration.

Biochemistry 48:33 (2009) 7979-7985

Authors:

D Spetzler, R Ishmukhametov, T Hornung, LJ Day, J Martin, WD Frasch

Abstract:

Increases in the power stroke and dwell durations of single molecules of Escherichia coli F(1)-ATPase were measured in response to viscous loads applied to the motor and inhibition of ATP hydrolysis. The load was varied using different sizes of gold nanorods attached to the rotating gamma subunit and/or by increasing the viscosity of the medium using PEG-400, a noncompetitive inhibitor of ATPase activity. Conditions that increase the duration of the power stroke were found to cause 20-fold increases in the length of the dwell. These results suggest that the order of hydrolysis, product release, and substrate binding may change as the result of external load on the motor or inhibition of hydrolysis.