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Nat Methods 2004 Dec 18;1(3):209-17. Epub 2004 Nov 18.

Department of Pharmacology, University of Colorado Health Sciences Center, Aurora, Colorado 80045, USA.

Nearly every major process in a cell is carried out by assemblies of multiple dynamically interacting protein molecules. To study multi-protein interactions within such molecular machineries, we have developed a fluorescence microscopy method called three-chromophore fluorescence resonance energy transfer (3-FRET). This method allows analysis of three mutually dependent energy transfer processes between the fluorescent labels, such as cyan, yellow and monomeric red fluorescent proteins. Read More

Indian J Exp Biol 2007 Jan;45(1):48-57

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

Microscopy has become an essential tool for cellular protein investigations. The development of new fluorescent markers such as green fluorescent proteins generated substantial opportunities to monitor protein-protein interactions qualitatively and quantitatively using advanced fluorescence microscope techniques including wide-field, confocal, multiphoton, spectral imaging, lifetime, and correlation spectroscopy. The specific aims of the investigation of protein dynamics in live specimens dictate the selection of the microscope methodology. Read More

Methods Cell Biol 2008 ;89:569-98

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

Förster resonance energy transfer (FRET) is an effective and high resolution method to monitor protein-protein interactions in live or fixed specimens. FRET can be used to estimate the distance between interacting protein molecules in vivo or in vitro using laser-scanning confocal FRET microscopy. The spectral overlap of donor and acceptor-essential for FRET-also generates a contamination of the FRET signal, which should be removed in order to carry out quantitative data analysis with confidence. Read More

Cytometry A 2003 May;53(1):39-54

Flow Cytometry Section, Office of Science and Technology, National Institute of Arthritis and Musculosketal and Skin Diseases/NIH, 9000 Rockville Pike, Building 10, Room 9N228, Bethesda, MD 20892, USA.

Background: Use of distinct green fluorescent protein (GFP) variants permits the study of protein-protein interactions and colocalization in viable transfected cells by fluorescence (Förster) resonance energy transfer (FRET). Flow cytometry is a sensitive method to detect FRET. However, the typical dual-laser methods used in flow cytometric FRET assays are not generally applicable because they require a specialized krypton ultraviolet (UV) laser. Read More