Three-color Förster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time.

@article{Ernst2012ThreecolorFR,
  title={Three-color F{\"o}rster resonance energy transfer within single F₀F₁-ATP synthases: monitoring elastic deformations of the rotary double motor in real time.},
  author={Stefan Ernst and Monika G. D{\"u}ser and Nawid Zarrabi and Michael B{\"o}rsch},
  journal={Journal of biomedical optics},
  year={2012},
  volume={17 1},
  pages={
          011004
        }
}
Catalytic activities of enzymes are associated with elastic conformational changes of the protein backbone. Förster-type resonance energy transfer, commonly referred to as FRET, is required in order to observe the dynamics of relative movements within the protein. Förster-type resonance energy transfer between two specifically attached fluorophores provides a ruler with subnanometer resolution between 3 and 8 nm, submillisecond time resolution for time trajectories of conformational changes… 
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Background Citations
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Methods Citations
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TLDR
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TLDR
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TLDR
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The regulatory switch of F1-ATPase studied by single-molecule FRET in the ABEL trap
TLDR
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Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases
TLDR
The enzyme’s rotary progression during ATP hydrolysis is monitored by three single-molecule techniques: fluorescence video-microscopy with attached actin filaments, Förster resonance energy transfer between pairs of fluorescence probes, and a polarization assay using gold nanorods, and it is found that one dwell in the three-steppedrotary progression lasting longer than the other two by a factor of up to 1.6.
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