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Yellow fluorescent protein, Zoanthus Yellow fluorescent protein ( YFP ) is a genetic mutant of green fluorescent protein (GFP) originally derived from the jellyfish Aequorea victoria . [ 1 ] Its excitation peak is 513 nm and its emission peak is 527 nm. [ 2 ]
The widely used iGluSnFR consists of a circularly permuted enhanced green fluorescent protein (cpEGFP) fused to a glutamate binding protein (GluBP) from a bacterium. [3] When GluBP binds a glutamate molecule, it changes its shape, pulling the EGFP barrel together, increasing fluorescence.
The FAST-fluorogen reporting system is used to explore the living world, from protein reporting (e.g., for protein trafficking), protein-protein interaction monitoring (and a number of biosensors), to chemically induced dimerization. It is implemented in fluorescence microscopy, flow cytometry and any other fluorometric methods.
Fluorescent proteins include: Green fluorescent protein (GFP) Yellow fluorescent protein (YFP) Red fluorescent protein (RFP)
A simplified Jablonski diagram illustrating the change of energy levels.. The principle behind fluorescence is that the fluorescent moiety contains electrons which can absorb a photon and briefly enter an excited state before either dispersing the energy non-radiatively or emitting it as a photon, but with a lower energy, i.e., at a longer wavelength (wavelength and energy are inversely ...
GFP catalyzes the oxidation and only requires molecular oxygen. GFP has been modified by changing the wavelength of light absorbed to include other colors of fluorescence. YFP or yellow fluorescent protein, BFP or blue fluorescent protein, and CFP or cyan fluorescent protein are examples of GFP variants. These variants are produced by the ...
The C-terminal end of Channelrhodopsin-2 extends into the intracellular space and can be replaced by fluorescent proteins without affecting channel function. This kind of fusion construct can be useful to visualize the morphology of ChR2 expressing cells, i.e. simultaneously indicate which cells are tagged with FP and allow the activity to be ...
In molecular biology, the PYP domain (photoactive yellow protein) is a p-coumaric acid-binding protein domain. They are present in various proteins in bacteria. PYP is a highly soluble globular protein with an alpha/beta fold structure. It is a member of the PAS domain superfamily, which also contains a variety of other kinds of photosensory ...
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