Subunit rotation in single FRET-labeled F1-ATPase hold in solution by an anti-Brownian electrokinetic trap

@inproceedings{Sielaff2013SubunitRI,
  title={Subunit rotation in single FRET-labeled F1-ATPase hold in solution by an anti-Brownian electrokinetic trap},
  author={Hendrik Sielaff and Thomas Heitkamp and Andrea Zappe and Nawid Zarrabi and Michael Boersch},
  booktitle={Photonics West - Biomedical Optics},
  year={2013}
}
FoF1-ATP synthase catalyzes the synthesis of adenosine triphosphate (ATP). The F1 portion can be stripped from the membrane-embedded Fo portion of the enzyme. F1 acts as an ATP hydrolyzing enzyme, and ATP hydrolysis is associated with stepwise rotation of the γ and ε subunits of F1. This rotary motion was studied in great detail for the last 15 years using single F1 parts attached to surfaces. Subunit rotation of γ was monitored by videomicroscopy of bound fluorescent actin filaments, nanobeads… 
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