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Energy transfer fluorescence

Fluorescence energy transfer is the transfer of electronic energy from a molecule in an excited state (donor) to another molecule (acceptor). The efficiency of this process is dependent on the distance between the donor and the acceptor. The fluorescence energy transfer process may or may not lead to emission of fluorescence by the acceptor. The transfer is due to [Pg.248]

The fluorescence energy transfer process has been widely used to determine the distance between fluorophores, the surface density of fluorophores in the lipid bilayer, and the orientation of membrane protein or protein segments, often with reference to the membrane surface and protein-protein interactions. Membranes are intrinsically dynamic in nature, so that so far the major applications have been the determination of fixed distances between molecules of interest in the membrane. [Pg.249]

In this section we will briefly outline the theory of fluorescence energy transfer as applied to the study of the more simple case of the surface distribution of acceptor and donor in the same plane. A number of theories for interpretation of fluorescence energy transfer data have been developed for more complex situations which cannot be elaborated here due to space limitations however, these are referred to where appropriate. [Pg.249]

Another process which can occur during the excited state is fluorescence energy transfer, which is the transfer of the excited state energy from a donor (D) to an acceptor (A) (Fig. 4). The transfer is called radiation-less because it occurs without the appearance of a photon. This process is strongly dependent upon distance because it is the result of dipole-dipole coupling between the donor and the acceptor [16]. A requirement for energy transfer is that the emission spectrum of the donor overlaps with the absorption spectrum of the acceptor. The rate of transfer (A ) is given by [Pg.9]

Usually, both the transfer efficiency (E) and Rq are determined experimentally. Then, the donor-to-acceptor distance is calculated using [Pg.10]

This method is widely used to measure the distance between sites on a macromolecule, and has been the subject of considerable experimentation and discussion [17-19], [Pg.10]

Energy transfer has been used to measure the self-association of melittin. The melittin was labeled with a Af-methylanthraniloyl (NMA) residue on one of the lysine residues. This fluorophore serves as the energy acceptor for the single tryptophan residue. Only a small fraction (5%) of the melittin monomers was labeled with NMA. In the monomer there is only one tryptophan residue near the acceptor, whereas four such residues are present in the tetramer. Hence, the extent of tryptophan to NMA energy transfer should be sensitive to and increased by melittin self-association. In this experiment the intention is not to determine a distance, but rather to use the association-dependent energy transfer to determine the extent of self-association [20]. [Pg.10]

Emission spectra of the labeled melittin are shown in Fig. 9. Recall that only a small fraction of the melittin contains a NMA label. Hence, the emission spectra are mostly characteristic of tryptophan, with shoulders at 430 nm due to the NMA emission. In the presence of 2 M NaCl the NMA emission is enhanced, reflecting [Pg.11]


Brockhinke, A. and Linne, M.A., Short-pulse techniques Picosecond fluorescence, energy transfer and "quench-free" measurements, in Applied Combustion Diagnostics, Kohse-Hoinghaus, K. and Jeffries, J.B. (Eds.), Taylor Francis, New York, 2002, Chapter 5. [Pg.12]

Intramolecular distances determined by fluorescence energy transfer... [Pg.98]

Dorn, 1. T., Neumaier, K. R. and Tampe, R. (1998) Molecular recognition of histidine-tagged molecules by metal-chelating lipids monitored by fluorescence energy transfer and correlation spectroscopy. ]. Am. Chem. Soc 120, 2753. [Pg.153]

Amler, E., A. Abbott and W. J. Ball, Structural dynamics and oligometric interactions of Na+,K+-ATPase as monitored using fluorescence energy transfer, Biophys. J., 61, 553 (1992). [Pg.464]

Other supramolecular structures such as dendrimers have also been synthesized with zinc-containing porphyrins. Sixteen free base and sixteen zinc porphyrin units were added at the fifth generation of dendritic poly(L-lysine) and intramolecular fluorescence energy transfer was observed.823 Assembly of supramolecular arrays in the solid state has been achieved with the incorporation of an amide group for hydrogen bonding. Zinc meso-tetra(4-amidophenyl)porphyrin... [Pg.1219]

Gershkovich AA, Kholodovych W (1996) Fluorogenic substrates for proteases based on intramolecular fluorescence energy transfer (IFETS). J Biochem Biophys Methods 33 135-162... [Pg.23]

Sq635-b and Sq660 were also utilized as donor-acceptor pairs in combination with an HSA/anti-HSA system, in a fluorescence energy transfer (FRET)-based immunoassay [95, 96]. [Pg.86]

Oswald B, Lehmann F, Simon L, Terpetschnig E, Wolfbeis OS (2000) Red laser-induced fluorescence energy transfer in an immunosystem. Anal Biochem 280 272-277... [Pg.103]

Fluorescence energy transfer experiments, in which the energy transfer from the excited DNA bases to a fluorescent ligand is monitored by fluorescence excitation spectroscopy, has been used to analyze the binding of the bisquinolizinium species 35 to DNA <2004ARK219>. [Pg.9]

Stryer, L. (1978). Fluorescence energy transfer as a spectroscopic ruler. Annu. Rev. Biochem. 47, 819—46. [Pg.63]

Oswald, B., Lehmann, F., Simon, L., Terpetschnig, E. and Wolfbeis, O. S. (2000). Red laser-induced fluorescence energy transfer in an immunosys-tem. Anal. Biochem. 280, 272-7. [Pg.65]

Young, R., Arnette, J., Roess, D. and Barisas, B. (1994). Quantitation of fluorescence energy transfer between cell surface proteins via fluorescence donor photobleaching kinetics. Biophys. J. 67, 881-8. [Pg.70]

Li, Y. L. and Glazer, A. N. (1999). Design, synthesis, and spectroscopic properties of peptide-bridged fluorescence energy-transfer cassettes. Bioconjug. Chem. 10, 241-245. [Pg.293]

Matsuoka, K., Nishimura, S. I. and Lee, Y. C. (1995). A bi-fluorescence-labeled substrate for ceramide glycanase based on fluorescence energy-transfer. Carbohydr. Res. 276, 31-42. [Pg.297]

Verbist, J., Gadella, T. W. J., Raeymaekers, L., Wuytack, F., Wirtz, K. W. A. and Casteels, R. (1991). Phosphoinositide-protein Interactions of the plasma-membrane Ca2+-transport ATPase as revealed by fluorescence energy-transfer. Biochim. Biophys. Acta 1063, 1-6. [Pg.299]

Isaacs, B.S., Husten, E.J., Esmon, C.T., and Johnson, A.E. (1986) A domain of membrane-bound blood coagulation factor Va is located far from the phospholipid surface. A fluorescence energy transfer measurement. Biochemistry 25, 4958-4969. [Pg.1077]

Khanna, P.L., and Ullman, E.F. (1980) 4, 5 -dimethoxy-6-carboxyfluorescein A novel dipole-dipole coupled fluorescence energy transfer acceptor useful for fluorescence immunoassays. Anal. Biochem. 108,156. [Pg.1082]

Woo F1Y, Vak D, Korystov D, Mikhailovsky A, Bazan GC, Kim DY (2007) Cationic conjugated polyelectrolytes with molecular spacers for efficient fluorescence energy transfer to dye-labeled DNA. Adv Funct Mater 17 290-295... [Pg.451]

Thomas D. D., Carlsen W. F. and Stryer L. (1978) Fluorescence Energy Transfer in the Rapid-Diffusion Limit, Proc. Nat. Acad. Sci. 75, 5746-5750. [Pg.272]

An immunosensor based on a competitive fluorescence energy-transfer immunoassay was reported by Anderson 105) for the measurement of phenytoin. Texas red-labeled antibody was incubated with a phenytoin derivative. On displacement of the derivative by the antigen, the change in the fluorescence signal was recorded. Detection limits approached 5 /iM with response times ranging from 5 to 30 min. [Pg.213]

D. Meadows and J. S. Schultz, Fiber-optic biosensors base on fluorescence energy transfer, Talanta 35, 145-150 (1988). [Pg.333]

L. M. Christian and W. R. Seitz, An optical ionic-strength sensor based on polyelectrolyte association and fluorescence energy transfer, Talanta 35, 119-122 (1988)... [Pg.333]

Z. Zhang, W. R. Seitz, and K. O Connel, Amylase substrate based on fluorescence energy transfer, Anal. Chim. Acta 236, 251-256 (1988). [Pg.333]

Figure 14.18. Diagrammatic representation of a phenytoin fluorescence energy transfer fiber optic sensor, as described in the text. -< = Antibody-Texas Red P = unlabeled phenytoin P = phenytoin-b-phyco-erythrin. (Adapted from Ref, 119.)... Figure 14.18. Diagrammatic representation of a phenytoin fluorescence energy transfer fiber optic sensor, as described in the text. -< = Antibody-Texas Red P = unlabeled phenytoin P = phenytoin-b-phyco-erythrin. (Adapted from Ref, 119.)...

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Energy transfer fluorescence measurements

Energy transfer long-range fluorescence

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