Structural highlights
Function
A0A182DW87_ECOLX
Publication Abstract from PubMed
Forster 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.
A Guide to Fluorescent Protein FRET Pairs.,Bajar BT, Wang ES, Zhang S, Lin MZ, Chu J Sensors (Basel). 2016 Sep 14;16(9). pii: E1488. doi: 10.3390/s16091488. PMID:27649177[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bajar BT, Wang ES, Zhang S, Lin MZ, Chu J. A Guide to Fluorescent Protein FRET Pairs. Sensors (Basel). 2016 Sep 14;16(9). pii: E1488. doi: 10.3390/s16091488. PMID:27649177 doi:http://dx.doi.org/10.3390/s16091488
