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  2. Förster resonance energy transfer - Wikipedia

    en.wikipedia.org/wiki/Förster_resonance_energy...

    Jablonski diagram of FRET with typical timescales indicated. The black dashed line indicates a virtual photon.. Förster resonance energy transfer (FRET), fluorescence resonance energy transfer, resonance energy transfer (RET) or electronic energy transfer (EET) is a mechanism describing energy transfer between two light-sensitive molecules (chromophores). [1]

  3. Methods to investigate protein–protein interactions - Wikipedia

    en.wikipedia.org/wiki/Methods_to_investigate...

    Label transfer can be used for screening or confirmation of protein interactions and can provide information about the interface where the interaction takes place. Label transfer can also detect weak or transient interactions that are difficult to capture using other in vitro detection strategies. In a label transfer reaction, a known protein ...

  4. Time-resolved fluorescence energy transfer - Wikipedia

    en.wikipedia.org/wiki/Time-resolved_fluorescence...

    Excitation of the donor fluorophore (in this case, the lanthanide ion complex) by an energy source (e.g. flash lamp or laser) produces an energy transfer to the acceptor fluorophore if they are within a given proximity to each other (known as the Förster's radius). The acceptor fluorophore in turn emits light at its characteristic wavelength.

  5. Bimolecular fluorescence complementation - Wikipedia

    en.wikipedia.org/wiki/Bimolecular_fluorescence...

    Fluorescence resonance energy transfer , also known as förster resonance energy transfer, resonance energy transfer or electronic energy transfer , is based on the transfer of energy from an excited chromophore or fluorophore (if the chromophores are fluorescent) to a nearby acceptor. In this method, fluorophores are chemically linked or ...

  6. Single-molecule FRET - Wikipedia

    en.wikipedia.org/wiki/Single-molecule_FRET

    Single-molecule fluorescence (or Förster) resonance energy transfer (or smFRET) is a biophysical technique used to measure distances at the 1-10 nanometer scale in single molecules, typically biomolecules. It is an application of FRET wherein a pair of donor and acceptor fluorophores are excited and detected at a single molecule level. In ...

  7. Direct analysis in real time - Wikipedia

    en.wikipedia.org/wiki/Direct_analysis_in_real_time

    Eluate from a high-pressure liquid chromatograph can be also introduced to the reaction zone of the DART source and analyze. DART can be coupled with capillary electrophoresis (CE) and the eluate of CE is guided to the mass spectrometer through the DART ion source. [1]

  8. Isoelectric focusing - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_focusing

    The buffer solution in each vessel has an electrical contact with a voltage divider connected to a high-voltage power supply, which establishes an electrical field along the capillary. When a sample (a mixture of peptides or proteins) is injected in the capillary, the presence of the electrical field and the pH gradient separates these ...

  9. High-resolution transmission electron microscopy - Wikipedia

    en.wikipedia.org/wiki/High-resolution...

    High-resolution transmission electron microscopy is an imaging mode of specialized transmission electron microscopes that allows for direct imaging of the atomic structure of samples. [ 1 ] [ 2 ] It is a powerful tool to study properties of materials on the atomic scale, such as semiconductors, metals, nanoparticles and sp 2 -bonded carbon (e.g ...