The green fluorescent protein or GFP which was first isolated from Aequorea Victoria (jellyfish species), is able to give off green colour fluorescent light when illuminated with ultraviolet light (UV).Green Fluorescence is produced naturally in Aequorea Victoria when calcium binds to a protein, aequorin causing it to release blue light. This blue light is then absorbed by GFP and emitted as green light. 
GFP from Aequorea Victoria has an excitation peaks at wavelengths of 395nm and 475nm where the GFP absorbs light causing its electrons to become excited and emit green light at 509nm.
GFP is 26.9kDa in size and has a unique beta-can structure made of 11 beta-strands which forms a beta-barrel with an alpha-helix running through the center. The chromophore (a p-hydroxybenzylideneimidazolinone) which is responsible for the fluorescent property of GFP is formed from residues 65–67, which are Ser-Tyr-Gly in native GFP.
GFP can be used in applications such as biomarkers or bioreporters where the GFP gene could be incorporated into genes encoding for proteins and be translated out together with the protein of interest. This allows the location and the movement of the protein to be detected. This can serve to be a useful tool as it allows us to determine what are the protein’s target site in the body or when they are made. Another advantage that GFP possess is that unlike other small fluorescent molecules used previously, GFPs are less harmful to living cells when illuminated. Hence GFP is a valuable marker of gene expression.
References
GFP from Aequorea Victoria has an excitation peaks at wavelengths of 395nm and 475nm where the GFP absorbs light causing its electrons to become excited and emit green light at 509nm.(Left-Topology of GFP; Right-GFP Structure with Chromophore in the center)
GFP is 26.9kDa in size and has a unique beta-can structure made of 11 beta-strands which forms a beta-barrel with an alpha-helix running through the center. The chromophore (a p-hydroxybenzylideneimidazolinone) which is responsible for the fluorescent property of GFP is formed from residues 65–67, which are Ser-Tyr-Gly in native GFP.
GFP can be used in applications such as biomarkers or bioreporters where the GFP gene could be incorporated into genes encoding for proteins and be translated out together with the protein of interest. This allows the location and the movement of the protein to be detected. This can serve to be a useful tool as it allows us to determine what are the protein’s target site in the body or when they are made. Another advantage that GFP possess is that unlike other small fluorescent molecules used previously, GFPs are less harmful to living cells when illuminated. Hence GFP is a valuable marker of gene expression.References
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