User:Vincent de Chavez/Sandbox 1
From Proteopedia
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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 that occurs within the <scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization2/1'>Ser65, Tyr66, and Gly67 </scene>residues. | 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 that occurs within the <scene name='User:Vincent_de_Chavez/Sandbox_1/Cyclization2/1'>Ser65, Tyr66, and Gly67 </scene>residues. | ||
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| + | <scene name='User:Vincent_de_Chavez/Sandbox_1/Testtowork/1'>TextToBeDisplayed</scene> | ||
Revision as of 05:00, 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 that occurs within the residues.
