Inside Cover: Homo‐FRET Imaging as a Tool to Quantify Protein and Lipid Clustering (ChemPhysChem 3/2011)

Bader, Arjen N.; Hoetzl, Sandra; Hofman, Erik; Voortman, Jarno; Henegouwen, Paul M.P. van Bergen en; Meer, Gerrit van; Gerritsen, Hans C.

doi:10.1002/cphc.201190012

Cited by 1 publication

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“…Theoretical descriptions which do not take these features into proper account (e.g., Yeow and Clayton, 2007) should be viewed cautiously. Despite this complexity, homo-FRET is still regularly used in membrane studies, more recently in combination with fluorescence microscopy (see section below and Table 1; Bader et al, 2011) to detect and characterize chromophore (e.g., labeled protein) confinement or aggregation. In this regard, it should be noted that the use of high numerical aperture objectives results in reduction of the observed anisotropy (Axelrod, 1979).…”

Section: Homo-fret Vs Hetero-fretmentioning

confidence: 99%

FRET in membrane biophysics: an overview

Loura

Prieto²

2011

Front. Physio.

109

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Förster resonance energy transfer (FRET), in most applications used as a “spectroscopic ruler,” allows an easy determination of the donor-acceptor intermolecular distance. However, the situation becomes complex in membranes, since around each donor there is an ensemble of acceptors at non-correlated distances. In this review, state-of-the-art methodologies for this situation are presented, usually involving time-resolved data and model fitting. This powerful approach can be used to study the occurrence of phase separation (“rafts” or other type of domains), allowing their detection as well as size evaluation. Formalisms for studying lipid–protein and protein–protein interactions according to specific topologies are also addressed. The advantages and added complexity of a specific type of FRET (energy homotransfer or energy migration) are described, as well as applications of FRET under the microscope.

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Section: Homo-fret Vs Hetero-fretmentioning

confidence: 99%