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.
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Acknowledgements
The authors thank Dr. Claire E. Atkinson for critical reading of the manuscript. This work was supported by NIH grant 1RO1CA142858 awarded to A.I.M. and NIH grant 1R21AR066920 awarded to A.L.M.
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Mattheyses, A.L., Marcus, A.I. (2015). Förster Resonance Energy Transfer (FRET) Microscopy for Monitoring Biomolecular Interactions. In: Meyerkord, C., Fu, H. (eds) Protein-Protein Interactions. Methods in Molecular Biology, vol 1278. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2425-7_20
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DOI: https://doi.org/10.1007/978-1-4939-2425-7_20
Publisher Name: Humana Press, New York, NY
Print ISBN: 978-1-4939-2424-0
Online ISBN: 978-1-4939-2425-7
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