User:Nargiza Mahmudova/Sandbox 1
From Proteopedia
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Three mutations on the beta barrel of the Green Fluorescent Protein, F99S, M153T and V163A, causes this specific mutant to fluoresce much greater than the wild type protein. As a result it serves as a better marker for gene expression in vivo. | Three mutations on the beta barrel of the Green Fluorescent Protein, F99S, M153T and V163A, causes this specific mutant to fluoresce much greater than the wild type protein. As a result it serves as a better marker for gene expression in vivo. | ||
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==Background== | ==Background== | ||
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| + | Green Fluorescent Protein (GFP) was acquired from the luminescent Aequorea victoria jellyfish. Wild type GFP is a 238 amino acid protein and the fluorescent choromophore is formed by an internal cyclization of a Serine-Tyrosine-Glycine tripeptide. GFP absorbs blue light primarily at 395 nm accompanied by a smaller peak at 475 nm and emits green light at 509 nm with a smaller peak at 540 nm. The Green Fluorescent Protein has been used as a reporter protein for gene expression, protein localization and cell linage information. The slow rate of fluorescence attainment in vivo limits the GFP as a reporter for gene expression. Considerable variations of GFP have been created in order to help determine the structure and function of the wtGFP. These mutations have been made in order to enhance the use of GFP as a reporter of gene regulation and expression, protein transport, and heredity. GFP has been mutated to provide an increased or alternative color for fluorescence, for a greater time period and to make it less susceptible to photo bleaching. The specific GFP mutation model featured is referred to as Mutant F99S/M153T/V163A or cycle 3 GFP (c3-GFP). | ||
Revision as of 20:04, 15 March 2009
Mutant F99S/M153T/V163A - c3-GFP
Three mutations on the beta barrel of the Green Fluorescent Protein, F99S, M153T and V163A, causes this specific mutant to fluoresce much greater than the wild type protein. As a result it serves as a better marker for gene expression in vivo.
Background
Green Fluorescent Protein (GFP) was acquired from the luminescent Aequorea victoria jellyfish. Wild type GFP is a 238 amino acid protein and the fluorescent choromophore is formed by an internal cyclization of a Serine-Tyrosine-Glycine tripeptide. GFP absorbs blue light primarily at 395 nm accompanied by a smaller peak at 475 nm and emits green light at 509 nm with a smaller peak at 540 nm. The Green Fluorescent Protein has been used as a reporter protein for gene expression, protein localization and cell linage information. The slow rate of fluorescence attainment in vivo limits the GFP as a reporter for gene expression. Considerable variations of GFP have been created in order to help determine the structure and function of the wtGFP. These mutations have been made in order to enhance the use of GFP as a reporter of gene regulation and expression, protein transport, and heredity. GFP has been mutated to provide an increased or alternative color for fluorescence, for a greater time period and to make it less susceptible to photo bleaching. The specific GFP mutation model featured is referred to as Mutant F99S/M153T/V163A or cycle 3 GFP (c3-GFP).
