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.