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	Fluorescence resonance energy transfer - Wikipedia, the free encyclopedia
		is the fluorescence quantum yield of the donor in the absence of the acceptor, and J is the spectral overlap integral calculated as
		In fluorescence microscopy, fluorescence confocal laser scanning microscopy, as well as in molecular biology, FRET is a useful tool to quantify molecular dynamics in biophysics, such as protein-protein interactions, protein-DNA interactions, and protein conformational changes.
		A limitation of FRET is the requirement for external illumination to initiate the fluorescence transfer, which can lead to background noise in the results from direct excitation of the acceptor, or photobleaching.
	en.wikipedia.org /wiki/Fluorescence_resonance_energy_transfer (1012 words)

	Fluorescence - Wikipedia, the free encyclopedia
		Fluorescence is a luminescence that is mostly found as an optical phenomenon in cold bodies, in which a molecule absorbs a high-energy photon, and re-emits it as a lower-energy photon with a longer wavelength.
		Fluorescence is named after the mineral fluorite, composed of calcium fluoride, which exhibits this phenomenon.
		Fluorescence has been used to study the structure and conformations of DNA and proteins with techniques such as Fluorescence resonance energy transfer.
	en.wikipedia.org /wiki/Fluorescence (992 words)

	Fluorescense Resonance Energy Transfer
		FRET (Fluorescence Resonance Energy Transfer) is a technique for measuring interactions between two proteins in vivo.
		This eliminates the energy transfer from donor to acceptor and should cause an increase in the emission from the donor (due to the fact that it is not transferring energy to the acceptor).
		The physics of the FRET energy transfer between donor and acceptor (which is non-radiative) is such that the efficiency falls off with the sixth power of the distance between molecules.
	www.iscid.org /encyclopedia/Fluorescense_Resonance_Energy_Transfer (556 words)

	Olympus FluoView Resource Center: FRET Introductory Concepts
		Fluorescence resonance energy transfer is a process by which radiationless transfer of energy occurs from an excited state fluorophore to a second chromophore in close proximity.
		Resonance energy transfer is not sensitive to the surrounding solvent shell of a fluorophore, and thus, produces molecular information unique to that revealed by solvent-dependent events, such as fluorescence quenching, excited-state reactions, solvent relaxation, or anisotropic measurements.
		Because fluorescence resonance energy transfer requires the donor and acceptor molecules to have the appropriate dipole alignment and be positioned within 10 nanometers of each other, the tertiary structure of the reagents to which the molecules are attached must be considered.
	www.olympusfluoview.com /applications/fretintro.html (7876 words)

	Invitrogen - Molecular Probes - Note 1.2 - Technical Focus: Fluorescence Resonance Energy Transfer (FRET) (Site not responding. Last check: 2007-10-03)
		Fluorescence resonance energy transfer (FRET) is a distance-dependent interaction between the electronic excited states of two dye molecules in which excitation is transferred from a donor molecule to an acceptor molecule without emission of a photon.
		When FRET is used as a contrast mechanism, colocalization of proteins and other molecules can be imaged with spatial resolution beyond the limits of conventional optical microscopy.
		Schematic representation of the FRET spectral overlap integral.
	probes.invitrogen.com /handbook/boxes/0422.html (379 words)

	Fluorescence Resonance Energy Transfer Microscopy (FRETM) (Site not responding. Last check: 2007-10-03)
		Fluorescence can be used as a spectroscopic ruler to study and quantify the interactions of cellular components on the molecular level.
		Fluorescence resonance energy transfer is a process by which a fluorophore (donor) in an excited state may transfer its excitation energy to a neighboring chromophore (acceptor) nonradiatively through dipole-dipole interactions.
		The usefulness of this technique derives from the fact that the efficiency of the energy transfer process varies as the inverse of the sixth power of the distance separating the donor and acceptor fluorophores, resulting in the ability to measure interactions between cellular components on a scale of 10-50Å.
	www-cellbio.med.unc.edu /facilities/fret.htm (396 words)

	Definition of Fluorescence resonance energy transfer
		where $\kappa^2 is the dipole orientation factor, n is the refractive index of the medium, Q_0 is the$ fluorescence quantum yield of the donor in the absence of the acceptor, and $J is the spectral overlap integral calculated as$
		In fluorescence microscopy, fluorescence confocal laser scanning microscopy, as well as in molecular biology, FRET is a useful biophysical tool to quantify molecular dynamics, such as protein-protein interactions, protein-DNA interactions, and protein conformational changes.
		FRET is also a common tool in the study of reaction kinetics.
	www.wordiq.com /definition/Fluorescence_resonance_energy_transfer (758 words)

	Fluorescence Resonance Energy Transfer (Site not responding. Last check: 2007-10-03)
		FRET (Fluorescence Resonance Energy Transfer) is a photophysical effect where energy that is absorbed by one fluorescent molecule (donor) is transferred non-radiatively to a second fluorescent molecule (acceptor).
		An increase of FRET leads to a decrease in donor emission and an increase of acceptor emission.
		Protein A is excited by absorbing light of 440 nm and transfers the energy to protein B. Now protein B is excited and falls back to its ground-state, thereby emitting light at 520 nm.
	www.chem.tue.nl /smo/MBE/FRET.htm (257 words)

	M. Aigle - Use of GFP mutants as probe for protein-protein interactions through fluorescence resonance energy transfer ... (Site not responding. Last check: 2007-10-03)
		The FRET phenomenon, that we are developping, consists in a fluorescence transfer between a donor and a receptor fluorochromes.
		FRET can then be used for in vitro monitoring a complex between two yeast proteins.
		Use of FRET for in vitro visualization of this complex is in progress.
	www.yeastgenome.org /yeast96/f3016.html (258 words)

	FRET Page
		Kt is the rate of energy transfer(radiationless), hve, hvd and hva are the photon energies of the donor excitation, of the donor fluorescence and of the acceptor fluorescence.
		The donor quantum yield in the presence of transfer (Qda) and in the absence of transfer (Qd) are
		The solid curve represents the relationship between the efficiency of the fluorescence resonance energy transfer and the distance separating the donor and the acceptor.
	www.anatomy.usyd.edu.au /mru/fret/abot.html (932 words)

	Olympus FluoView Resource Center: Confocal Microscope Product Information - Fluorescence Resonance Energy Transfer
		Note that for observation of energy transfer between CFP and YFP, simultaneous excitation must be conducted at 442 and 515 nanometers.
		An example of FRET in HeLa cells is provided in the image to the right for ratio changes when cameleon is manifested on the HeLa cell and stimulated by histamine, and then inhibited by cyproheptadine.
		Energy transfer between CFP and YFP is proportional to bound calcium.
	www.olympusfluoview.com /products/fretproducts.html (471 words)

	Paul Selvin, UIUC Physics (Site not responding. Last check: 2007-10-03)
		Using LRET, Professor Selvin has detected single fluorescent molecules, their polarization states, spectra, and energy transfer between a single donor-acceptor pair via confocal and near-field scanning optical microscopy, produced time-resolved microscopic images of lanthanide chelates, showed that europium has an unexpected emission polarization, and used picosecond fluorescence spectroscopy to detect anharmonic torsional modes in DNA.
		FRET and LRET have the potential to greatly improve the quantitative nature of ion-channel measurements in living cells because they are a more direct measurement of physical distance than previous techniques.
		This resolution is achieved because the lanthanide can transfer energy to a suitably-chosen organic dye via a dipole-dipole mechanism that is sensitive to angstrom changes in distance between the two labels.
	www.physics.uiuc.edu /People/Faculty/profiles/Selvin (1099 words)

	Biophysical Journal: Fluorescence resonance energy transfer-based stoichiometry in living cells (Site not responding. Last check: 2007-10-03)
		Present microscopic methods measure FRET in arbitrary units, and cannot discriminate FRET efficiency and the fractions of donor and acceptor in complex.
		Here we describe a stoichiometric method that uses three microscopic fluorescence images to measure FRET efficiency, the relative concentrations of donor and acceptor, and the fractions of donor and acceptor in complex in living cells.
		A second equation determines the fraction of donor molecules in complex by estimating the donor fluorescence lost due to energy transfer.
	www.findarticles.com /p/articles/mi_qa3938/is_200212/ai_n13572329 (717 words)

	Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes -- ... (Site not responding. Last check: 2007-10-03)
		the intensity of the fluorescence of the donor fluorophore decreases.
		Dashed arrows indicate the magnitude of the decrease in TET fluorescence that occurs when the TET-labeled strands are hybridized to the TMR-labeled strand, and solid arrows indicate the magnitude and direction of the change in TMR fluorescence that occurs when the TET-labeled strands are hybridized to the TMR-labeled strand.
		The fluorescence of the hybrid (open circles) was divided by the fluorescence of the FAM-labeled oligodeoxyribonucleotide alone (open squares), which decreases as the temperature is increased, in order to obtain the corrected fluorescence of the hybrid as a function of temperature (filled circles).
	nar.oupjournals.org /cgi/content/full/30/21/e122 (4071 words)

	Fluorescence Resources
		Fluorescence is a phenomenon that is used routinely in life science research.
		Fluorescence probes and conjugations are used extensively to trace the whereabouts of cellular components and protein localisation, it is used in fluorescence spectroscopy and a host of more complex applications (that give rise to great abbreviations) such as Fluorescence Resonance Energy Transfer (FRET), Fluorescence Recovery After Photobleaching (FRAP) and Fluorescence Activated Cell Sorting (FACS).
		Fluorescence Polarisation Guide provided in PDF format a comprehensive guide by PanVera describes receptor-ligand binding, immunoassays, DNA hybridization, theory of binding data analysis and more.
	www.fluorescence-resource.com (371 words)

	NPG web focus: imaging in cell biology : Review
		1a,b): the fluorescent protein must fold correctly to fluoresce, the host protein also needs to fold correctly to be functional, and the integrity of the chimeric protein must be maintained.
		The decision of whether to fuse a fluorescent protein to the amino or carboxyl terminus of a protein depends on the properties of the protein.
		It is also essential that the fluorophores fluoresce at a high efficiency and that the act of labelling does not disrupt the biochemical function or cellular localization of the host protein.
	www.nature.com /focus/cellbioimaging/content/full/ncb1031.html (4329 words)

	Fluorescence resonance energy transfer (FRET)
		The image of the Texas Red fluorescence reporting anti-carrot tubulin mAb1F8 (a) is highly similar to the image of the fluorescein fluorescence reporting affinity-purified anti-pp50 antibodies (b).
		These data indicate that the fluorescence observed in c is the result of FRET; i.e., the laser line used to excite anti-pp50-associated fluorochrome does not directly excite the anti-tubulin-associated fluorochrome.
		FRET suggests that some pp50 is very closely associated (i.e., 50 Å) with microtubules upon fixation, in turn, indicating that the pp50/microtubule co-localization observed in footprints lysed prior to fixation is not the result of an artifactual redistribution of pp50.
	www.geocities.com /ndurso/pr_6.htm (276 words)

	Robert M. Clegg
		We employ a variety of techniques, such as fluorescence spectroscopy, rapid kinetic methods and physical perturbations in order to probe the intra- and intermolecular interactions of these macromolecular structures, and to understand the physical basis of their biological functions.
		Fluorescence resonance energy transfer (FRET) is used for mapping the three-dimensional structures of biological macromolecules.
		The progression of the polymerase along a template can be followed by fluorescence, the rate of the reaction can be influenced by dye- and drug-binding to the template and RNA product, and the catalytic reaction steps can be tuned with pressure, temperature and small interacting molecular components.
	www.life.uiuc.edu /biochem/f_clegg.html (905 words)

	Wiley::Resonance Energy Transfer
		The resonance transfer of energy between molecules, or between sites within a large molecule, plays a central role in many areas of modern chemistry and physics.
		It is the first comprehensive modern survey of the field, offering a broad, yet detailed view of the mechanisms of energy transfer.
		The broad range of applications of fluorescence and fluorescence energy transfer to studies in molecular biology and biotechnology ensures that resonance energy transfer will be a vital component of the new science and technology of the next millenium.
	www.wiley.com /WileyCDA/WileyTitle/productCd-0471987328.html (256 words)

	Single Molecule Fluorescence Resonance Energy Transfer (FRET)
		Well, it is usually impossible to detect single biomolecules directly so we use a simple trick of attaching a fluorescent dye molecule to a well-defined position on a host molecule.
		Since fluorescence signal is red-shifted relative to the excitation light, we can use optical filters to reject the scattered laser light and achieve almost backgroun-free detection of single molecules.
		FRET is measured between two dyes, donor and acceptor.
	bio.physics.uiuc.edu /newTechnique.html (415 words)

	DNA Tetraplex Formation Studied with Fluorescence Resonance Energy Transfer -- Simonsson and Sjöback 274 (24): ... (Site not responding. Last check: 2007-10-03)
		Fluorescence resonance energy transfer (FRET) is a process by which the excited state energy of a fluorescent donor chromophore
		The fluorescence resonance energy transfer efficiency in the 27-base-long oligonucleotide fluorescein-5'-d(TGG GGA GGG TGG GGA GGG TGG GGA AGG)-3'-tetramethyl rhodamine depends on the nature of the cation.
		FRET as a suitable tool to study tetraplex formation.
	www.jbc.org /cgi/content/full/274/24/17379 (3461 words)

	Fluorescence Resonance Energy Transfer-Based Stoichiometry in Living Cells -- Hoppe et al. 83 (6): 3652 -- Biophysical ... (Site not responding. Last check: 2007-10-03)
		Fluorescence Resonance Energy Transfer-Based Stoichiometry in Living Cells -- Hoppe et al.
		by estimating the donor fluorescence lost due to energy transfer.
		FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells
	www.biophysj.org /cgi/content/abstract/83/6/3652 (633 words)

	MPIbpc 25 Years - Molecular Biology
		Functional characteristics of DNA transcription and the structure of the nucleosome organization within chromosomes are studied on a molecular level by high pressure and fluorescence techniques.
		(1994) Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer.
		EMBO J. 15: 4246-53; Jares-Erijman, E.A., and Jovin, T.M. (1996) Determination of DNA helical handedness by fluorescence resonance energy transfer.
	www.mpibpc.gwdg.de /inform/25years/Jovin.html (623 words)

	Fluorescence Resonance Energy Transfer, FP-FRET
		Fluorescence Resonance Energy Transfer (FRET) occurs when the emission of one fluorophore overlaps the absorbance of a second fluorophore and is proportional to their intermolecular distance (for review, see Wu and Brand, Analytical Biochem, 218, 1-13, 1994).
		If the donor fluorophore is excited with the appropriate wavelength of light, the result is quenching of its emission and indirect excitation and emission from the acceptor fluorophore.
		Developed in the laboratory of Dr. Roger Tsien at UCSD (Miyawaki et al, Nature, 388, 882-887, 1977), FRET using GFP spectral mutants provides the ability to localize and monitor non-binding and molecular protein-protein interaction in living cells.
	www.glenspectra.co.uk /glen/filters/fret.htm (121 words)

	Development of a baculovirus-based fluorescence resonance energy transfer assay for measuring protein-protein ... (Site not responding. Last check: 2007-10-03)
		Development of a baculovirus-based fluorescence resonance energy transfer assay for measuring protein-protein interaction -- Cheung and Hearn 270 (24): 4973 -- FEBS Journal
		Development of a baculovirus-based fluorescence resonance energy transfer assay for measuring protein–protein interaction
		FRET was enhanced by the addition of a GnRH agonist but not
	www.ejbiochem.org /cgi/content/abstract/270/24/4973 (317 words)

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