Forster resonance energy transfer properties

The lifetime of the excited state of fluorophores may be altered by physical and biochemical properties of its environment. Fluorescence lifetime imaging microscopy (FLIM) is thus a powerful analytical tool for the quantitative mapping of fluorescent molecules that reports, for instance, on local ion concentration, pH, and viscosity, the fluorescence lifetime of a donor fluorophore, Forster resonance energy transfer can be also imaged by FLIM. This provides a robust method for mapping protein-protein interactions and for probing the complexity of molecular interaction networks. 

We have developed the splinted RNA ligation procedure outlined in this chapter to generate site-specifically dye-labeled telomerase RNA constructs. These modified telomerase RNA constructs may be used to characterize dynamic RNA structural properties using Forster resonance energy transfer (FRET) (Stone et al., 2007). Our laboratory specializes in single molecule FRET measurements, which facilitates the direct observation of transient RNA structural states. The details of single molecule FRET... 

There is much to do in this direction, both for exploiting new intermediates, as is the case for the recently rapidly developing aryl cation chemistry (by irradiation of aryl chlorides and related reagents) and by a more extensive exploitation of their properties. A collected book on Forster resonance energy transfer has been published, and refers to a very active topic. ... 

The theory of resonance transfer of electronic excitation energy between donor and acceptor molecules of suitable spectroscopic properties was first presented by Forster.(7) According to this theory, the rate constant for singlet energy transfer from an excited donor to a chromophore acceptor which may or may not be fluorescent is proportional to r 6, where r is the distance... 

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