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Cytometry of Fluorescence Resonance Energy Transfer

2004
Publisher Summary luorescence resonance energy transfer (FRET) is a phenomenon in fluorescence spectroscopy where energy is transferred from an excited donor molecule to an acceptor molecule under favorable spectral, proximity, and orientational conditions.
János Szöllosi   +2 more
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Fluorescence resonance energy transfer

Current Opinion in Biotechnology, 1995
In the past year, a number of studies have demonstrated the utility of fluorescence resonance energy transfer as a technique for probing complex intermolecular interactions and for determining the spatial extension and geometrical characteristics of multicomponent structures composed of diverse molecular constituents, such as proteins, lipids ...
openaire   +3 more sources

Plasmon‐Enhanced Fluorescence Resonance Energy Transfer

The Chemical Record, 2019
AbstractIn this review, we firstly introduce physical mechanism of fluorescence resonance energy transfer (FRET), the methods to measure FRET efficiency, and the applications of FRET. Secondly, we introduce the principle and applications of plasmon‐enhanced fluorescence (PEF).
Xinxin Wang   +5 more
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Fluorescence resonance energy transfer sensors

Research on Chemical Intermediates, 2001
We describe the various implementations of fluorescence resonance energy transfer with respect to the kinetic design principles involved in fluorescence lifetime sensors. Applications to metal ion and glucose detection are discussed. The versatility and key developments for using timecorrelated single-photon counting in fluorescence lifetime based ...
Birch, D.J.S., Rolinski, O.J.
openaire   +3 more sources

Ultrafast fluorescence resonance energy transfer in a micelle

The Journal of Chemical Physics, 2006
Ultrafast fluorescence resonance energy transfer (FRET) from coumarin 153 (C153) to rhodamine 6G (R6G) is studied in a neutral PEO20–PPO70–PEO20 triblock copolymer (P123) micelle and an anionic micelle (sodium dodecyl sulfate, SDS) using a femtosecond up-conversion setup.
Kankan Bhattacharyya   +6 more
openaire   +3 more sources

Nonextensive kinetics of fluorescence resonance energy transfer

The Journal of Chemical Physics, 2008
Some fluorescence dyes in complex media, such as those found in biology, demonstrate nonextensive kinetics, which implies representing their fluorescence decays in terms of lifetime distributions rather than simple exponentials. Complex kinetics usually discourage application to lifetime sensors, as it is believed, that additional molecular mechanisms ...
Rolinski, O.J., Birch, D.J.S.
openaire   +4 more sources

Single-Molecule Fluorescence Resonance Energy Transfer [PDF]

open access: possibleMethods, 2001
Fluorescent resonance energy transfer (FRET) is a powerful technique for studying conformational distribution and dynamics of biological molecules. Some conformational changes are difficult to synchronize or too rare to detect using ensemble FRET. FRET, detected at the single-molecule level, opens up new opportunities to probe the detailed kinetics of ...
openaire   +2 more sources

The renaissance of fluorescence resonance energy transfer.

Nature structural biology, 2000
Recent advances in fluorescence resonance energy transfer have led to qualitative and quantitative improvements in the technique, including increased spatial resolution, distance range, and sensitivity. These advances, due largely to new fluorescent dyes, but also to new optical methods and instrumentation, have opened up new biological applications.
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[13] Fluorescence resonance energy transfer

1995
Publisher Summary Fluorescence resonance energy transfer (FRET) is a technique for measuring the distance between two points which are separated by approximately 10–75 A°. The technique is valuable because measurements can be made under physiological (or other) conditions with near angstrom resolution and with the exquisite sensitivity of ...
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Fluorescence Resonance Energy Transfer Microscopy (FRET)

2014
FRET (Förster Resonance Energy Transfer) microscopy breaks the resolution limit of light to let us investigate the conformation and function of proteins within living cells. Intensity-based methods are the most popular and direct approach to detect FRET.
Kees Jalink, Katarzyna M. Kedziora
openaire   +3 more sources

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