A Guide to Fluorescent Protein FRET Pairs

By Bryce T. Bajar, Emily S. Wang, Shu Zhang, Michael Z. Lin, Jun Chu. Italian National Conference on Sensors, 2016

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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.

Subfields: Biophysics, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7012dd84c7e2a85fac92c23f7f6c046649515204

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Citations in the corpus

• Fluorescence lifetime imaging microscopy: fundamentals and advances in instrumentation, analysis, and applications (2020, background): “Finally, FLIM-FRET and multiexponential fitting can be used to quantify the proportion of quenched and unquenched donor molecules.(18) FRET events can be confirmed by photobleaching the acceptor, which should result in a donor lifetime at pre-FRET levels.”