Single-molecule observations of turnover, co-operativity and mechanochemistry in a macromolecular complex

Dr. Richard BerryDepartment of Physics, Clarendon Lab, Oxford, United Kingdom
Tuesday 27 July, Location: MRC-LMCB, time: 17:15

The bacterial flagellar motor has long been a canonical macromolecular complex because of the relative ease with which its output, rotation of the extracellular flagellar filament, can be observed.  In vivo imaging of GFP-labelled components of the motor has revealed that the motor is not a static structure, but that individual proteins are constantly replaced at rates on the order of 1/minute.  Localization at nanometre precision of labels attached to the motor, at frame rates of several to many kilohertz, has also allowed observations of the mechanism of co-operative directional switching in the motor and of its mechanochemical cycle.

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