Monitoring subunit rotation in single FRET-labeled FoF1-ATP synthase in an anti-Brownian electrokinetic trap

@inproceedings{Heitkamp2013MonitoringSR,
  title={Monitoring subunit rotation in single FRET-labeled FoF1-ATP synthase in an anti-Brownian electrokinetic trap},
  author={Thomas Heitkamp and Hendrik Sielaff and Anja Korn and Marc Renz and Nawid Zarrabi and Michael Boersch},
  booktitle={Photonics West - Biomedical Optics},
  year={2013}
}
FoF1-ATP synthase is the membrane protein catalyzing the synthesis of the 'biological energy currency' adenosine triphosphate (ATP). The enzyme uses internal subunit rotation for the mechanochemical conversion of a proton motive force to the chemical bond. We apply single-molecule Förster resonance energy transfer (FRET) to monitor subunit rotation in the two coupled motors F1 and Fo. Therefore, enzymes have to be isolated from the plasma membranes of Escherichia coli, fluorescently labeled and… 
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