From Proteopedia
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- | This [[Help:Sandboxes|Sandbox]] page is available for temporary practice work. Nothing in a ''Sandbox'' page is permanent. You may prefer to create your own personal Sandbox page -- see [[Help:Getting Started in Proteopedia|instructions]]. Feel free to add practice content below this paragraph, or delete everything below this paragraph, but please do not delete this paragraph.
| + | Practice on adding '''green links''' |
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- | <Structure load='3tnu' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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- | <scene name='Sandbox/Acidic_residues/1'>Acidic residues</scene>
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- | <scene name='Sandbox/Basic_residues/1'>Basic residues</scene>
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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.
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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 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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- | [[2b7a]]
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- | <Structure load='1ema' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
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Revision as of 16:36, 23 April 2013
Practice on adding green links