Sandbox 736
From Proteopedia
(Difference between revisions)
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
== Example page for GFP == | == Example page for GFP == | ||
| - | <StructureSection load='1ema' size='300' side='right' caption='Structure of GFP (PDB entry [[1ema]])' scene=''>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. | + | <StructureSection load='1ema' size='300' side='right' caption='Structure of GFP (PDB entry [[1ema]])' scene=''> |
| + | |||
| + | |||
| + | [[Image:1ema.gif.gif|thumb|left|350px|Green Flourescent Protein (1ema)|]] | ||
| + | |||
| + | |||
| + | 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. | ||
| Line 6: | Line 12: | ||
| - | GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='56/563149/Cromo/1'>chromophore</scene>, 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 | + | GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The <scene name='56/563149/Cromo/1'>chromophore</scene>, 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>. |
| + | .</StructureSection> | ||
| + | |||
| + | == Reference == | ||
| + | <references/> | ||
| + | |||
| + | |||
| + | |||
| + | == Quiz == | ||
| + | <quiz display=simple> | ||
| + | {How many alpha helices are in this structure?} | ||
| + | -One | ||
| + | -None | ||
| + | + Eleven | ||
| + | - Twelve | ||
| + | </quiz> | ||
Current revision
Example page for GFP
| |||||||||||
Reference
- ↑ 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
