Sandbox dov 21

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<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
<applet load='1ema' size='300' frame='true' align='right' caption='Insert caption here' />
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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 <scene name='Sandbox_dov_21/Highlight_chromophore/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.
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<scene name='Sandbox_dov_21/Aricept_mov/1'>TextToBeDisplayed</scene>

Revision as of 07:17, 26 July 2009

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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Drag the structure with the mouse to rotate


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