User:Shai Biran/GFP test page
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| - | == | + | == Your Heading Here (maybe something like 'Structure') == |
<StructureSection load='1ema' size='300' frame='true' side='right' caption='GFP ([[1ema]])' scene=''> | <StructureSection load='1ema' size='300' frame='true' side='right' caption='GFP ([[1ema]])' scene=''> | ||
[[Image:1ema.gif|thumb|left|450px|Green fluorescent protein (1ema)]] | [[Image:1ema.gif|thumb|left|450px|Green fluorescent protein (1ema)]] | ||
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Exploring the Structure | Exploring the Structure | ||
| - | GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The | + | 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.<ref>PMID:8703075</ref> |
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</StructureSection> | </StructureSection> | ||
Current revision
Your Heading Here (maybe something like 'Structure')
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References
- ↑ Ormo M, Cubitt AB, Kallio K, Gross LA, Tsien RY, Remington SJ. Crystal structure of the Aequorea victoria green fluorescent protein. Science. 1996 Sep 6;273(5280):1392-5. PMID:8703075
