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SPECIAL SECTION ON FRONTIERS IN MICROSCOPY

Fluorescence resonance energy transfer microscopy: a mini review

[+] Author Affiliations
Ammasi Periasamy

University of Virginia, W. M. Keck Center for Cellular Imaging, Department of Biology, Gilmer Hall, Charlottesville, Virginia 22904

J. Biomed. Opt. 6(3), 287-291 (Jul 01, 2001). doi:10.1117/1.1383063
History: Received Mar. 19, 2001; Accepted Apr. 3, 2001
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Fluorescence resonance energy transfer (FRET) microscopy is a better method than the x-ray diffraction, nuclear magnetic resonance, or electron microscopy for studying the structure and localization of proteins under physiological conditions. In this paper, we describe four different light microscopy techniques to visualize the interactions of the transcription factor CAATT/enhancer binding protein alpha (C/EBPα) in living pituitary cells. In wide-field, confocal, and two-photon microscopy the FRET image provides two-dimensional spatial distribution of steady-state protein–protein interactions. The two-photon imaging technique provides a better FRET signal (less bleedthrough and photobleaching) compared to the other two techniques. This information, although valuable, falls short of revealing transient interactions of proteins in real time. The fluorescence lifetime methods allow us to monitor FRET signals at the moment of the protein interactions at a resolution on the order of subnanoseconds, providing high temporal, as well as spatial resolution. This paper will provide a brief review of the above-mentioned FRET techniques.© 2001 Society of Photo-Optical Instrumentation Engineers.

© 2001 Society of Photo-Optical Instrumentation Engineers

Citation

Ammasi Periasamy
"Fluorescence resonance energy transfer microscopy: a mini review", J. Biomed. Opt. 6(3), 287-291 (Jul 01, 2001). ; http://dx.doi.org/10.1117/1.1383063


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