Forster resonance energy transfer FRET

Forster resonance energy transfer—FRET what is it, why do it, and how it s done... 

There are numerous excellent reviews and original literature about Forster resonance energy transfer (FRET) where one can read detailed descriptions and get lists of earlier references [1-11]. This chapter is neither a review of the literature, nor a detailed account... 

Fluorescence or Forster resonance energy transfer (FRET) is widely accepted as being one of the most useful methods to observe biochemical events in vitro and in living cells. Generally, there are two forms of FRET sensors those based on a pair of genetically encoded fluorophores, usually employing fluorescent proteins from jellyfish or corals, or those based on small molecules that make use of small organic fluorophores. 

Forster resonance energy transfer (FRET) is a form of quenching. For a fluorophore (donor) to be quenched by another molecule (acceptor), three criteria must be met ... 

A detailed theory of energy transfer by the Coulombic mechanism was developed by Forster, so the process is often referred to as Forster resonance energy transfer (FRET). According to the Forster theory, the probability of Coulombic energy transfer falls off inversely with the sixth power of the distance between the donor and the acceptor. For... 

Fluorescence (or Forster) resonance energy transfer (FRET) is a process by which energy is transferred nonradiatively from an excited donor to a nearby ground state acceptor. This process arises due to dipole-dipole interactions and is... 

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... 

Fluorescence (or Forster) resonance energy transfer (FRET) (Forster, 1948 Perrin, 1932) provides a spectroscopic way of estimating distances over a size range that is appropriate for biological macromolecules. It is based upon fluorescence, one of the most sensitive spectroscopic methods. Fluorescence is the emission of light from an excited molecule, having lost... 

QDs have been also used extensively as efficient donors in the development of Forster resonance energy transfer (FRET) systems. The key developments and most recent applications in chemical analysis using such QDs-based strategies are reviewed below. 

Figure 16.25 Semiconductor nanoparticle-based fluorescent sensors (a) Forster resonant energy transfer (FRET) between two nanoparticles induced by analyte, (b) crown ether receptor for potassium ions, and (c) operation principle of maltose fluorescent sensor. (Adapted from Chen et at. [144] and Medintz et at. [146])...

Forster Resonance Energy Transfer (FRET) for Proteins... 

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