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Donor (D) and acceptor (A) molecule which participate in FRET (Förster resonance energy transfer).

What is FRET with FLIM (FLIM-FRET)?

This article explains the FLIM-FRET method which combines resonance energy transfer and fluorescence lifetime imaging to study protein-protein interactions.

Transverse histological cut of a rabbit tongue. 50 Mpixels images (2326 µm x 1739 µm) in 14 x 18 tiles. Lifetime gives an additional contrast that allows to differentiate different structures in histological stainings.

A Guide to Fluorescence Lifetime Imaging Microscopy (FLIM)

The fluorescence lifetime is a measure of how long a fluorophore remains on average in its excited state before returning to the ground state by emitting a fluorescence photon.

Step by Step Guide for FRAP Experiments

Fluorescence Recovery After Photobleaching (FRAP) has been considered the most widely applied method for observing translational diffusion processes of macromolecules. The resulting information can be…

Fluorescence Correlation Spectroscopy (FCS)

Fluorescence correlation spectroscopy (FCS) measures fluctuations of fluorescence intensity in a sub-femtolitre volume to detect such parameters as the diffusion time, number of molecules or dark…

Fluorescence Recovery after Photobleaching (FRAP) and its Offspring

FRAP (Fluorescence recovery after photobleaching) can be used to study cellular protein dynamics: For visualization the protein of interest is fused to a fluorescent protein or a fluorescent dye. A…

Förster Resonance Energy Transfer (FRET)

The Förster Resonance Energy Transfer (FRET) phenomenon offers techniques that allow studies of interactions in dimensions below the optical resolution limit. FRET describes the transfer of the energy…