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Fluorescence fluctuation technique reveals stoichiometry

Gary Boas

Förster resonance energy transfer (FRET) can offer tremendous insight into protein interactions inside cells. However, it typically does not provide quantitative information about the protein complex, telling the researcher only that interactions have occurred. Fluorescence correlation spectroscopy offers a possible alternative, but quantitative interpretation with the technique is difficult. In the Feb. 27 issue of PNAS, investigators with the University of Minnesota, Minneapolis, reported a method based on fluorescence fluctuation spectroscopy that enabled them to measure quantitatively...Read full article

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    Published: May 2007
    Glossary
    förster resonance energy transfer
    Förster resonance energy transfer (FRET) is a mechanism describing the transfer of energy between two closely spaced fluorescent molecules. This phenomenon is named after the German scientist Theodor Förster, who first described it in the context of dipole-dipole interactions between molecules. In FRET, two fluorophores (molecules that fluoresce, or emit light, upon excitation) are involved: a donor and an acceptor. The donor fluorophore absorbs a photon and, instead of emitting a...
    BiophotonicscellsFörster resonance energy transferMicroscopyResearch & Technologyspectroscopy

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