Resonance Forster energy transfer

Ag Antigen FRET Forster resonance energy transfer... 

Forster, Th 211, 278, 282, 285 Forster resonance energy transfer, 282 Forster singlet energy transfer, 378 Franck-Condon factors, 23 Franck-Condon principle, 5 Franck-Condon transition, 5 French, C. S., 555 Friedman, G., 353 Fritzsche, J., 37 Frosch, R. P 252, 267, 269 Fumaronitrile, photodimerization in solid state, 478... 

Hildebrandt N, Charbonniere LJ, Lohmannsroben HG (2007) Time-resolved analysis of a highly sensitive forster resonance energy transfer immunoassay using terbium complexes as donors and quantum dots as acceptors. J Biomed Biotechnol 2007 79169... 

Liao F, Xie Y, Yang X et al (2009) Homogeneous noncompetitive assay of protein via Forster-resonance-energy-transfer with tryptophan residue(s) as intrinsic donor(s) and fluorescent ligand as acceptor. Biosens Bioelectron 25 112-117... 

Day RN, Booker CF, Periasamy A (2008) Characterization of an improved donor fluorescent protein for Forster resonance energy transfer microscopy. J Biomed Opt 13 031203. doi 10.1117/1111.2939094... 

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... 

Hickerson, R., Majumdar, Z. K., Baucom, A., Clegg, R. M. and Noller, H. F. (2005). Measurement of internal movements within the 30 S ribosomal subunit using Forster resonance energy transfer. J. Mol. Biol. 354, 459-72. 

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. 

Ganesan, S., Ameer-Beg, S. M., Ng, T. T., Vojnovic, B. and Wouters, F. S. (2006). A dark yellow fluorescent protein (YFP)-based Resonance Energy-Accepting Chromoprotein (REACh) for Forster resonance energy transfer with GFP. Proc. Natl. Acad. Sci. USA 103, 4089-94. 

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. 

Spectral imaging and its use in the measurement of Forster resonance energy transfer in living cells... 

Pelet, S., Previte, M. J. and So, P. T. (2006). Comparing the quantification of Forster resonance energy transfer measurement accuracies based on intensity, spectral, and lifetime imaging. J. Biomed. Opt. 11, 34017. 

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 ... 

Eggeling, C., Widengren, J., Brand, L., Schaffer, J., Felekyan, S. and Seidel, C. A. (2006). Analysis of photobleaching in single-molecule multicolor excitation and Forster resonance energy transfer measurements. J. Phys. Chem. A 110, 2979-95. 

Posokhov, Y. O., Merzlyakov, M., Hristova, K. and Ladokhin, A. S. (2008). A simple proximity correction for Forster resonance energy transfer efficiency determination in membranes using lifetime measurements. Anal. Biochem. 380, 134—6. 

Clapp, A. R. Medintz, I. L. Mattoussi, H., Forster resonance energy transfer investigations using quantum dot fluorophores, Chemphyschem 2006, 7, 47 57... 

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... 

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