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Unformatted text preview: I ntroduction In 1962, Shimomura, Johnson, and Saiga, discovered and isolated the green fluorescent protein (GFP) in Aequoria jellyfish which have been in existence for over 160 million years. Shimomura et al were able to figure out which part of GFP was responsible for its fluorescent property. Since this discovery, several researchers have been able to clone and advance the understandings of proteins. With the help of GFP and its fluorescent property, researchers were able to attach GFP to a protein of interest and see when it was made and where it will go after being produced. GFP is a fairly small protein composed of 238 amino acids. I ts structure is a unique soda can shape (Figure 1). The – barrel is made up of 11 – strands and an – helix that runs through the center. β β α The chromophore is also located in the middle of the – barrel and is responsible for GFP’s β fluorescence. In the chromophore structure, the R groups are the first 64 and last 174 residues of GFP (Figure 2). residues of GFP (Figure 2)....
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- Spring '08
- Biology, Green fluorescent protein, Shimomura