Forster resonance energy transfer measurements

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. 

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. 

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. 

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

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. 

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... 

While the complementary technique Forster resonant energy transfer (FRET), which is widely used for studying distances in proteins requires two different, relatively large chromophores, which must be chosen according to the expected distance, EPR distance measurements can be performed using two identical much smaller nitroxide labels and are precise over a broad range of distances [51,65,66]. 

Second, we present a Forster resonance energy transfer (FRET) imaging method, which has been used to monitor GPGR-mediated dissociation (activation) and reassociation (deactivation) of heterotrimeric G-protein in single live cells (10, 11). Protein/protein interactions cannot be measured by colocalization of the proteins because the limit of resolution of the light microscope using standard techniques is on the order of hundreds of nanometers, and one cannot be certain that two proteins of interest physically interact even... 

Forster (1968) points out that R0 is independent of donor radiative lifetime it only depends on the quantum efficiency of its emission. Thus, transfer from the donor triplet state is not forbidden. The slow rate of transfer is partially offset by its long lifetime. The importance of Eq. (4.4) is that it allows calculation in terms of experimentally measured quantities. For a large class of donor-acceptor pairs in inert solvents, Forster reports Rg values in the range 50-100 A. On the other hand, for scintillators such as PPO (diphenyl-2,5-oxazole), pT (p-terphenyl), and DPH (diphenyl hexatriene) in the solvents benzene, toluene, and p-xylene, Voltz et al. (1966) have reported Rg values in the range 15-20 A. Whatever the value of R0 is, it is clear that a moderate red shift of the acceptor spectrum with respect to that of the donor is favorable for resonant energy transfer. 

The elucidation of the structure, dynamics and self assembly of biopolymers has been the subject of many experimental, theoretical and computational studies over the last several decades. [1, 2] More recently, powerful singlemolecule (SM) techniques have emerged which make it possible to explore those questions with an unprecedented level of detail. [3-55] SM fluorescence resonance energy transfer (FRET), [56-60] in particular, has been established as a unique probe of conformational structure and dynamics. [26-55] In those SM-FRET experiments, one measures the efficiency of energy transfer between a donor dye molecule and an acceptor dye molecule, which label specific sites of a macromolecule. The rate constant for FRET from donor to acceptor is assumed to be given by the Forster theory, namely [59,61-64]... 

Forster s theory [1], has enabled the efficiency of EET to be predicted and analyzed. The significance of Forster s formulation is evinced by the numerous and diverse areas of study that have been impacted by his paper. This predictive theory was turned on its head by Stryer and Haugland [17], who showed that distances in the range of 2-50 nm between molecular tags in a protein could be measured by a spectroscopic ruler known as fluorescence resonance energy transfer (FRET). Similar kinds of experiments have been employed to analyze the structure and dynamics of interfaces in blends of polymers. 

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