Characterization of a spectrally diverse set of fluorescent proteins as FRET acceptors for mTurquoise2.

ABSTRACT: The performance of Förster Resonance Energy Transfer (FRET) biosensors depends on brightness and photostability, which are dependent on the characteristics of the fluorescent proteins that are employed. Yellow fluorescent protein (YFP) is often used as an acceptor but YFP is prone to photobleaching and pH changes. In this study, we evaluated the properties of a diverse set of acceptor fluorescent proteins in combination with the optimized CFP variant mTurquoise2 as the donor. To determine the theoretical performance of acceptors, the Förster radius was determined. The practical performance was determined by measuring FRET efficiency and photostability of tandem fusion proteins in mammalian cells. Our results show that mNeonGreen is the most efficient acceptor for mTurquoise2 and that the p

SUBMITTER: Mastop M 

PROVIDER: S-EPMC5607329 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature