Cos'è fret?

FRET is an acronym for Förster Resonance Energy Transfer, a physical phenomenon that occurs when two fluorophores (fluorescent molecules) are in close proximity. It is a non-radiative energy transfer process that involves the transfer of energy from an excited state donor fluorophore to an acceptor fluorophore through dipole-dipole interactions.

FRET is widely used in various fields of science, including molecular biology, biochemistry, and cell biology. It enables scientists to study molecular interactions, protein-protein interactions, and protein conformational changes in living cells and organisms.

One of the key applications of FRET is in fluorescence microscopy, where it is used to detect and quantify molecular interactions within cells. By tagging different molecules of interest with donor and acceptor fluorophores, researchers can measure the energy transfer efficiency and deduce the proximity or interaction between the labeled molecules.

FRET can also be used as a biosensing tool, allowing the detection of specific molecules or analytes. By designing FRET-based biosensors, scientists have been able to monitor cellular processes such as calcium ion concentration, pH levels, and enzyme activities in real-time.

Overall, FRET has revolutionized the way scientists study molecular interactions and dynamics, providing valuable insights into various biological processes. Its versatility and sensitivity make it an essential tool in the field of molecular and cellular biology.