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Fluorescent energy transfer, between

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]

J. M. Vanderkooi, A. Ierokomas, H. Nakamura, and A. Martonosi, Fluorescence energy transfer between Ca2+ transport ATPase molecule in artifical membranes, Biochemistry 16, 1262-1267 (1977). [Pg.267]

Iqbal, A., Arslan, S., Okumus, B., Wilson, T. J., Giraud, G., Norman, D. G., Ha, T., and Lilley, D. M. J. (2008b). Orientation dependence in fluorescent energy transfer between Cy3 and Cy5 terminally-attached to double-stranded nucleic acids. Proc. Natl. Acad. Sci. USA 105, 11176-11181. [Pg.184]

Horton, R.A. et al. 2007. A substrate for deubiquitinating enzymes based on time-resolved fluorescence energy transfer between terbium and yellow fluorescent protein. Anal. Biochem. 360, 138-143. [Pg.46]

Many of the crystals were prepared in the presence of azide, which is known to enhance the MgADP inhibition [17], and azide has been resolved in a crystal [38]. Thus, the mutually similar structures, including that of EFi [39] which was also prepared in the presence of azide, must all represent, basically, the MgADP-inhibited state. In this state, 7 is orientated at 80° [18], as in the 80° intermediate during active rotation. Fluorescence energy transfer between probes on a / and rotating 7 has indicated that, of the two active rotation intermediates at 0° and 80°, the crystal structures are much closer to the 80° intermediate [40]. At 80°, we expect one catalytic site to be open to the medium (asterisks in Fig. 14.2B), which is consistent with the idea that the crystal structures with a fully open catalytic site mimic the 80° state rather than the ATP-waiting state. [Pg.281]

A very interesting application of local spectroscopy on the singlc-mol-ecule level was reported by Ha et al. [99], They investigated the fluorescence energy transfer between a pair of closely spaced dye molecules, one being... [Pg.41]

X 10 mol L range, with a detection limit of 0.27 jM. The fluorescence energy transfer between ferrocene donor and porphyrin acceptor was also considered. Nanofibers with distinct luminescent property were fabricated by electrospinning porphyrinated polyimides. The new material demonstrated to be a very interesting sensory material for detection of trace amounts of TNT vapor (10 ppb) [249]. The presence of covalently bonded porphyrin fluorophores in the main chain diminish the aggregation-induced self-quenching of fluorescence and improves the physicochemical stability of the polyimide nanofibers. [Pg.68]

The measurement of fluorescence intensity from a compound containing cliromophores of two spectral types is an example of a system for which it is reasonable to operate witli tire average rates of energy transfer between spectral pools of molecules. Let us consider tire simple case of two spectral pools of donor and acceptor molecules, as illustrated in figure C3.4.2 [18]. The average rate of energy transfer can be calculated as... [Pg.3020]

Miyawaki, A. and Tsien, R. (2000). Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol. 2000, 472-500. [Pg.66]

Klimov, V., Sekatskii, S. K. and Dietler, G. (2004). Coherent fluorescence resonance energy transfer between two dipoles Full quantum electrodynamics approach. J. Mod. Opt. 51, 1919 -7. [Pg.68]

Mitra, R. D., Silva, C. M. and Youvan, D. C. (1996). Fluorescence resonance energy transfer between blue-emitting and red-shifted excitation derivatives of the green fluorescent protein. Gene 173, 13-7. [Pg.231]

Selvin, P. R., Ha, T., Enderle, T., Ogletree, D. F., Chemla, D. S. and Weiss, S. (1996). Fluorescence resonance energy transfer between a single donor and a single acceptor molecule. Biophys. J. 70, Wp302-Wp302. [Pg.291]

Hering, V. R., Gibson, G., Schumacher, R. I., Faljoni-Alario, A. and Politi, M. J. (2007). Energy transfer between CdSe/ZnS core/shell quantum dots and fluorescent proteins. Bioconjug. Chem. 18, 1705-8. [Pg.525]

Clapp A.R., Mendintz I.L., Mauro J.M., Fisher B.R., Bawendi M.G., Mattoussi H. Fluorescence Resonance Energy Transfer Between Quantum Dot Donors and Dye-Labeled Protein Acceptors,./. Am. Chem. Soc. 2004 126 301-310. [Pg.116]

The sensor for the measurement of high levels of CO2 in gas phase was developed, as well90. It was based on fluorescence resonance energy transfer between 0 long-lifetime ruthenium polypyridyl complex and the pH-active disazo dye Sudan III. The donor luminophore and the acceptor dye were both immobilized in a hydrophobic silica sol-gel/ethyl cellulose hybrid matrix. The sensor exhibited a fast and reversible response to carbon dioxide over a wide range of concentrations. [Pg.373]


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