Information Panel

Measuring FRET by Sensitized Emission

This information panel was adapted from "Imaging Protein Interactions by FRET Microscopy," Chapter 32, in Protein-Protein Interactions (eds. Golemis and Adams). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY, USA, 2005.

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FRET, a nonradioactive, dipole-dipole coupling process, transfers energy from an excited donor fluorophore to an acceptor fluorophore in very close proximity (typically within 10 nm). Thus, excitation of the donor produces a sensitized emission from the acceptor that, in the absence of FRET, would not ordinarily occur, while simultaneously quenching the fluorescence of the donor. Proteins can be fused to genetically encoded GFP variants or chemically modified by covalent attachment of synthetic fluorophores, and the molecular interaction of the proteins in question can then be inferred by FRET between the fluorophores. The efficiency with which Förster-type energy transfer occurs in . . . [Full Text of this Article]