Sandbox Reserved 1236: Difference between revisions
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==Bioluminescent Structure Specifications== | ==Bioluminescent Structure Specifications== | ||
The attractive feature for the study and application of luciferase is its bioluminescent activity. The color of light produced has been found to vary depending on the organism that the protein is retrieved from. The fluorsence of light ranges through various wavelengths of light some of which include red, green and yellow light. This difference has a connection to the specificity of the active site of luciferase. Depending on the source of the protein different residues will produce a certain color of fluorescence. Variations in luciferase extracted from japanese fire flies has revealed this specificity. In high energy analogs of luciferase reveal the 286th residue is important in determine the color of light. When comparing green fluorescent japanese luciferin the active site contain an Ser286, while the red emitting variant has an Asp286. These findings indicate that slight variations in the active sight of luciferase can produce various effects on its bioluminencent activity. <ref>Goodsell, David . "Molecule of the Month: Luciferase." PDB-101: Luciferase. RSCB Protein Data Bank, June 2006. Web. 28 Apr. 2017.</ref> | The attractive feature for the study and application of luciferase is its bioluminescent activity. The color of light produced has been found to vary depending on the organism that the protein is retrieved from. The fluorsence of light ranges through various wavelengths of light some of which include red, green and yellow light. This difference has a connection to the specificity of the active site of luciferase. Depending on the source of the protein different residues will produce a certain color of fluorescence. Variations in luciferase extracted from japanese fire flies has revealed this specificity. In high energy analogs of luciferase reveal the 286th residue is important in determine the color of light. When comparing green fluorescent japanese luciferin the active site contain an Ser286, while the red emitting variant has an Asp286. These findings indicate that slight variations in the active sight of luciferase can produce various effects on its bioluminencent activity. <ref>Goodsell, David . "Molecule of the Month: Luciferase." PDB-101: Luciferase. RSCB Protein Data Bank, June 2006. Web. 28 Apr. 2017.</ref> | ||
[[Image:luciferase.png]] | |||
==Inhibitors== | ==Inhibitors== | ||