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Open AccessReview

A Guide to Fluorescent Protein FRET Pairs

1
Medical Scientist Training Program, University of California, Los Angeles, CA 90095, USA
2
Harvard College, Cambridge, MA 02138, USA
3
Institute of Biomedical and Health Engineering, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen 518055, China
4
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; https://doi.org/10.3390/s16091488
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)
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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MDPI and ACS Style

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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