User:Vincent de Chavez/Sandbox 1
From Proteopedia
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<scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization3/1'>test</scene> | <scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization3/1'>test</scene> | ||
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| - | <scene name='User:Vincent_de_Chavez/Sandbox_1/Test4/2'>this is a test</scene> | ||
{{Clear}} | {{Clear}} | ||
Revision as of 17:19, 9 March 2009
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GFP
Wild type green fluorescent protein consists of eleven antiparallel beta sheets that form a barrel around an internal alpha helix that runs along the axis of the barrel. The alpha helix contains the choromophore which is responsible for its fluorescence. The cyclization occurs within the residues, in which the amino group of Gly67 cylclizes with the carbonyl group of Ser65. In the presence of oxygen, Tyr66 is dehydrogenated which promotes the conjugated chromophore and its fluorescent properties.
