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Updated: Jun 6, 2026

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis
Published on: July 6, 2021
Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
1Third Institute of Physics, University of Stuttgart, Pfaffenwaldring 57, Stuttgart, Germany. m.boersch@physik.uni-stuttgart.de
Abstract:
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 F(o)F(1)-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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