Journal
BIOLOGICAL CHEMISTRY
Volume 392, Issue 1-2, Pages 135-142Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2011.001
Keywords
ABELtrap; anti-Brownian electrokinetic trap; FoF1-ATP synthase; fluorescence resonance energy transfer (FRET); single-molecule detection; subunit rotation
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Funding
- Deutsche Forschungsgemeinschaft [BO 1891/10-2]
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Conformational changes of proteins can be monitored in real time by fluorescence resonance energy transfer (FRET). Two different fluorophores have to be attached to those protein domains which move during function. Distance fluctuations between the fluorophores are measured by relative fluorescence intensity changes or fluorescence lifetime changes. The rotary mechanics of the two motors of FoF1-ATP synthase have been studied in vitro by single-molecule FRET. The results are summarized and perspectives for other transport ATPases are discussed.
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