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Sandbox dov 21

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(New page: 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 on...)
Current revision (09:14, 26 July 2009) (edit) (undo)
 
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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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Test of PyMOL-->JMol
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== Exploring the Structure ==
== Exploring the Structure ==
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<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
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<scene name='Sandbox_dov_21/Ache_lev/1'>AChE</scene>
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<scene name='Sandbox_dov_21/Ache_black/2'>AChE-Black</scene>
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<scene name='Sandbox_dov_21/Yechun/1'>Yechun-Scene</scene>
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<scene name='Sandbox_dov_21/Fas-ache/1'>FAS-AChE</scene>
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<scene name='Sandbox_dov_21/Z-dna_cartoon/2'>Z-DNA Cartoon</scene>
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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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<scene name='Sandbox_dov_21/Dots/1'>dots</scene>

Current revision

Test of PyMOL-->JMol

Exploring the Structure

Insert caption here

Drag the structure with the mouse to rotate


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