Fluorescence resonance energy transfer determination

B. J. Bacskai, J. Skoch, G.A. Hickey, R. Allen, B.T. Hyman, Fluorescence resonance energy transfer determinations using multiphoton fluorescence lifetime imaging microscopy to characterize amyloid-beta plaques, J. Biomed. Opt 8, 368-375 (2003)... 

Matyus, L. (1992) Fluorescence resonance energy transfer measurements on cell surfaces. A spectroscopic tool for determining protein interactions. J. Photochem. Photobiol. B Biol. 12, 323-337. 

Rolinski OJ, Birch DJS. Determination of acceptor distribution from fluorescence resonance energy transfer theory and simulation. J. Chem. Phys. 2000 112 8923-8933. 

Fluorescence resonance energy transfer (FRET) is a technique that has been used to measure distances between pairs of proximal fluorochromes. A suitable pair consists of a donor fluorochrome, which has an emission spectrum that significantly overlaps with the absorption spectrum of an acceptor fluorochrome (2). With the availability of monoclonal antibodies to many cell-surface determinants, intramolecular distances between nearby epitopes and intermolecular distances between adjacent cell-surface macromolecules can be investigated to analyze molecular interactions influencing important cellular events. Such monoclonal antibodies can be conjugated to fluorescein-isothiocyanate (FITC) as the donor, and either tetramethyl-rhodamine-isothiocyanate (TRITC) or phycoerythrin (PE) as the acceptor. 

Bullock GC> Bruns DE, Haverstick DM, Hepatitis C genotype determination by melting curve analysis with a single set of fluorescence resonance energy transfer probes. Clin Chem 2002 48 2147-54. 

The binding of synthetic ion channels and pores to lipid bilayer membranes often causes a change in intra- or intermolecular self-organization that is visible in sufficiently sensitive methods such as fluorescence (e.g. tryptophan emission) [14] or circular dichroism spectroscopy and can be used to determine the partition coefficient. Convenient methods of detection under relevant conditions are fluorescence resonance energy transfer (FRET) or fluorescence depth quenching (FDQ) [3, 4, 6]. Many fluorescent probes for the labeling of both synthetic ion channels/... 

Fluorescence resonance energy transfer (FRET) is another powerful technique for the determination of structural and functional information using fluorescent proteins. FRET is a physical phenomenon in which the distance between donor and acceptor fluorophores can be determined with reasonable accuracy [67]. This phenomenon was harnessed to study the c-Crk-II signaling protein, which is a substrate of the c-Abl protein kinase [68]. Using... 

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