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A Guide to Fluorescent Protein FRET Pairs

Medical Scientist Training Program, University of California, Los Angeles, CA 90095, USA
Harvard College, Cambridge, MA 02138, USA
Institute of Biomedical and Health Engineering, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China
Departments of Bioengineering and Neurobiology, Stanford University, CA 94305, USA
Author to whom correspondence should be addressed.
Academic Editors: Niko Hildebrandt, Igor Medintz and Russ Algar
Sensors 2016, 16(9), 1488;
Received: 21 July 2016 / Revised: 23 August 2016 / Accepted: 25 August 2016 / Published: 14 September 2016
(This article belongs to the Special Issue FRET Biosensors)
PDF [1939 KB, uploaded 14 September 2016]


Förster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution. Fluorescent proteins (FPs) are most commonly used as both donor and acceptor fluorophores in FRET biosensors, especially since FPs are genetically encodable and live-cell compatible. In this review, we will provide an overview of methods to measure FRET changes in biological contexts, discuss the palette of FP FRET pairs developed and their relative strengths and weaknesses, and note important factors to consider when using FPs for FRET studies. View Full-Text
Keywords: fluorescence resonance energy transfer (FRET); biosensors; fluorescent proteins fluorescence resonance energy transfer (FRET); biosensors; fluorescent proteins

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Bajar, B.T.; Wang, E.S.; Zhang, S.; Lin, M.Z.; Chu, J. A Guide to Fluorescent Protein FRET Pairs. Sensors 2016, 16, 1488.

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