Förster resonance energy transfer

What is Förster resonance energy transfer?
Example images
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Other experimental methods

What is Förster resonance energy transfer?

Förster resonance energy transfer (FRET) refers to the phenomenon where energy is non-radiatively transferred from an excited-state donor molecule to an acceptor molecule when two proteins are in close proximity. In the field of life sciences, this process is often associated with fluorescent molecules and is sometimes called Fluorescence resonance energy transfer.

The efficiency of FRET depends on factors such as the distance and angle between the molecules, as well as the spectral overlap. The distance at which the energy transfer efficiency is 50 % between the donor and acceptor is known as the Förster distance.

To measure FRET, for example, bind a fluorescent dye to protein A and protein B, one as a donor and the other as an acceptor, and measure the donor's or acceptor's fluorescence. When measuring the donor’s fluorescence, as the donor approaches the acceptor, the fluorescence intensity decreases. Conversely, when measuring the acceptor’s fluorescence, as the donor approaches the acceptor, the acceptor’s fluorescence intensity increases. By observing these changes in fluorescence intensity, you can study protein-protein interactions, including changes in distance and structure between the proteins.

Schematic diagram of intermolecular FRET

Figure 1: Schematic diagram of intermolecular FRET

Example images

Fast Ca²⁺ imaging of YC3.60 expressing HeLa cell

Data courtesy of Masahiro Nakano, Ph.D. and Takeharu Nagai, Ph.D. Department of Biomolecular Science and Engineering, The Institute of Scientific and Industrial Research, Osaka University

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