Sandbox 9
From Proteopedia
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| - | + | == Headline text == | |
| + | [[Image:1ema 9.gif|350px]] | ||
| + | Green fluorescent protein ('''GFP'''), originally isolated from the jellyfish Aequorea victoria (PDB entry [[1ema]]), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement. | ||
| - | == | + | == Exploring the Structure == |
| - | + | <applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here scene='Sandbox_9/Gfp/2'> | |
| - | Purine riboswitches are a class of riboswitches that selectively recognises guanine and become saturated at concentrations as low as 5 nM. In Bacillus subtilis, this mRNA motif is located on at least five separate transcriptional units that together encode 17 genes that are mostly involved in purine transport and purine nucleotide synthesis.[1] As some members of this family are also specific for adenine[3] or deoxyguanosine[4], this family are termed purine riboswitches. | ||
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| - | <scene name='Sandbox_9/ | + | '''GFP''' is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The chromophore, responsible for the fluorescent properties of the protein, is buried inside the beta barrel as part of the central alpha helix passing through the barrel. The chromophore forms via spontaneous cyclization and oxidation of three residues in the central alpha helix: -Thr65 (or Ser65)-Tyr66-Gly67. This cyclization and oxidation creates the chromophore's five-membered ring via a new bond between the threonine and the glycine residues. |
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| + | === Biological Significance === | ||
| + | '''GFP''' <scene name='Sandbox_9/Gfp/2'> GFP Chromophore </scene> is a useful marker protein that can be used for keeping track of gene expression in a tissue specific manner.<ref>PMID: 8703075 </ref> | ||
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| + | ==References== | ||
| + | <references/> | ||
Current revision
Headline text
Green fluorescent protein (GFP), originally isolated from the jellyfish Aequorea victoria (PDB entry 1ema), fluorsceses green (509nm) when exposed to blue light (395nm and 475nm). It is one of the most important proteins used in biological research because it can be used to tag otherwise invisible gene products of interest and thus observe their existence, location and movement.
Exploring the Structure
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