Fluorescence resonance energy transfer studies of protein interactions [PDF]
This thesis presents an investigation of fluorescence resonance energy transfer (FRET) as a reporting signal for protein-protein interactions. Quantitative optical assays to measure protein binding, conjugation and deconjugation are developed and results
Martin, Sarah Friede
core +2 more sources
Advanced Fluorescence Microscopy Techniques-FRAP, FLIP, FLAP, FRET and FLIM [PDF]
Fluorescence microscopy provides an efficient and unique approach to study fixed and living cells because of its versatility, specificity, and high sensitivity.
Ankerhold, Richard +5 more
core +1 more source
No better time to FRET: shedding light on host pathogen interactions [PDF]
Understanding the spatio-temporal subversion of host cell signaling by bacterial virulence factors is key to combating infectious diseases. Following a recent study by Buntru and co-workers published in BMC Biology, we review how fluorescence (Forster ...
Leong, J.M. +5 more
core +1 more source
Linear approaches to intramolecular Förster Resonance Energy Transfer probe measurements for quantitative modeling [PDF]
Numerous unimolecular, genetically-encoded Forster Resonance Energy Transfer (FRET) probes for monitoring biochemical activities in live cells have been developed over the past decade.
Kurt I. Anderson +24 more
core +1 more source
Structural Changes of Yellow Cameleon Domains Observed by Quantitative FRET Analysis and Polarized Fluorescence Correlation Spectroscopy [PDF]
Förster resonance energy transfer (FRET) is a widely used method for monitoring interactions between or within biological macromolecules conjugated with suitable donor-acceptor pairs.
Laptenok, S. +14 more
core +1 more source
Time-resolved FRET fluorescence spectroscopy of visible fluorescent protein pairs [PDF]
Förster resonance energy transfer (FRET) is a powerful method for obtaining information about small-scale lengths between biomacromolecules. Visible fluorescent proteins (VFPs) are widely used as spectrally different FRET pairs, where one VFP acts as a ...
Birch, D.J.S. +8 more
core +1 more source
The photoexcitation energy transfer is found and investigated in complexes of CdSe/ZnS cationic quantum dots and chlorin e6 molecules formed by covalent bonding and electrostatic interaction in aqueous solution and in porous track membranes.
Irina V. Martynenko +5 more
doaj +1 more source
FRET Ratiometric Nanoprobes for Nanoparticle Monitoring
Fluorescence labelling is often used for tracking nanoparticles, providing a convenient assay for monitoring nanoparticle drug delivery. However, it is difficult to be quantitative, as many factors affect the fluorescence intensity.
Guangze Yang +3 more
doaj +1 more source
A Guide to Fluorescent Protein FRET Pairs
Förster or fluorescence resonance energy transfer (FRET) technology and genetically encoded FRET biosensors provide a powerful tool for visualizing signaling molecules in live cells with high spatiotemporal resolution. Fluorescent proteins (FPs) are most
Bryce T. Bajar +4 more
doaj +1 more source
QTR-FRET: Efficient background reduction technology in time-resolved förster resonance energy transfer assays [PDF]
A novel homogeneous assay system QTR-FRET (Quencher modulated Time-Resolved Forster Resonance Energy Transfer) combining quenching resonance energy transfer (QRET) and time-resolved Forster resonance energy transfer (TR-FRET) was developed to reduce ...
Emmiliisa Vuorinen +5 more
core +1 more source

