User:Shai Biran/GFP test page

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(New page: == Example page for Green fluorescent protein ("GFP") == <StructureSection load='1ema' size='300' frame='true' side='right' caption='GFP (1ema)' scene=''> [[Image:1ema.gif|thumb|left|...)
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== Example page for Green fluorescent protein ("GFP") ==
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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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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.
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.
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== Exploring the Structure ==
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Exploring the Structure
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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The
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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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<scene name='Sandbox_4/Green_fp/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>
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</StructureSection>
</StructureSection>

Current revision

Your Heading Here (maybe something like 'Structure')

GFP (1ema)

Drag the structure with the mouse to rotate

References

  1. 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

Quiz

Points added for a correct answer:  
Points for a wrong answer:
Ignore the questions' coefficients:

1. How many alpha helics are in this structure?

One
None
Eleven
Twelve

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Shai Biran

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