Sandbox dav 4
From Proteopedia
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''ddddd'' deee dedee dede [[google.com/]] | ''ddddd'' deee dedee dede [[google.com/]] | ||
<Structure load='6OYH' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | <Structure load='6OYH' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /> | ||
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| - | ==Your Heading Here (maybe something like 'Structure')== | ||
| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | This is a default text for your page '''Google.com/'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
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| - | == Function == | ||
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| - | == Disease == | ||
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| - | == Relevance == | ||
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| - | == Structural highlights == | ||
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| - | This is a sample scene created with SAT to <scene name="/12/3456/Sample/1">color</scene> by Group, and another to make <scene name="/12/3456/Sample/2">a transparent representation</scene> of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes. | ||
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| - | </StructureSection> | ||
| - | == References == | ||
| - | <references/> | ||
Current revision
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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GFP is a beta barrel protein with 11 beta sheets. It is a 26.9kDa protein made up of 238 amino acids. The , 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 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
Mechanism
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Related 3D structures
ddddd deee dedee dede google.com/
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