User:Vincent de Chavez/Sandbox 1
From Proteopedia
(Difference between revisions)
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'''GFP''' | '''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 | + | 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 <scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization2/1'>Ser65, Tyr66, and Gly67 </scene>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. |
| - | <scene name='User:Vincent_de_Chavez/Sandbox_1/ | + | |
| + | |||
| + | <scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization3/1'>good</scene> | ||
Revision as of 15:16, 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.
