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Förster Resonance Energy Transfer (FRET) Microscopy for Monitoring Biomolecular Interactions

  • Alexa L. MattheysesEmail author
  • Adam I. Marcus
Part of the Methods in Molecular Biology book series (MIMB, volume 1278)

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.

Key words

Fluorescence FRET Sensitized emission Dynamics Microscopy Live cell imaging 

Notes

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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Copyright information

© Springer Science+Business Media New York 2015

Authors and Affiliations

  1. 1.Department of Cell BiologyEmory University School of MedicineAtlantaUSA
  2. 2.Department of Hematology and Medical OncologyWinship Cancer Institute of Emory UniversityAtlantaUSA

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