title: Förster resonance energy transfer (FRET) microscopy for monitoring biomolecular interactions.
abstract: Förster or Fluorescence resonance energy transfer (FRET) can be used to detect protein-protein interactions. When combined with microscopy, FRET has high temporal and spatial resolution, allowing the interaction dynamics of proteins within specific subcellular compartments to be detected in cells. FRET microscopy has become a powerful technique to assay the direct binding interaction of two proteins in vivo. Here, we describe a sensitized emission method to determine the presence and dynamics of protein-protein interactions in living cells.
authors: Department of Cell Biology, Emory University School of Medicine, Atlanta, GA, 30322, USA, mattheyses@emory.edu.
authors: Alexa L
authors: AL
authors: Mattheyses
authors: Adam I
authors: AI
authors: Marcus
mesh_terms: D002460:Cell Line; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D049452:Green Fluorescent Proteins / Q000737:chemistry; D006801:Humans; D008856:Microscopy, Fluorescence; D011485:Protein Binding; D025941:Protein Interaction Mapping; D060066:Protein Interaction Maps
chemical_list: D049452:Green Fluorescent Proteins