Time-Resolved Fluorescence Resonance Energy Transfer (TR-FRET) is a fluorescence based
technique which enables the analysis of molecular interactions in biochemical processes. Principle of
TR-FRET is based on time-resolved fluorescence (TRF) measurement and fluorescence resonance energy
transfer (FRET) between donor and acceptor molecules. To generate FRET signal, donor and acceptor
molecules must show spectral overlap and should be in close proximity to each other and display
suitable dipole orientation. The specific signal is acquired from molecules of interest via interactions of
donor and acceptor molecules. TR-FRET technique is widely used for studying kinase assays, cellular
signaling pathways, protein-protein interactions, DNA-protein interactions, and receptor-ligand binding.
There are various propriety applications of TR-FRET. Two different sample protocols are summarized
in this review.
Keywords: Biochemical processes, Time-Resolved Fluorescence, FRET, Förster resonance energy transfer.
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