Sandbox 1: Difference between revisions

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Student, Eran Hodis, Jaime Prilusky, Dan Bolser, Wayne Decatur, Filipe de Lima Pizzico, Annie Tomoe Takaesu

Revision as of 18:40, 20 February 2009 view source Student (talk \| contribs) students 33,697 edits No edit summary ← Older edit		Revision as of 18:59, 20 February 2009 view source Student (talk \| contribs) students 33,697 edits No edit summary Newer edit →
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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' />
	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.		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_1/Gfp_chromophore/2'>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.