This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
User:Vincent de Chavez/Sandbox 1
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
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. | ||
| + | |||
| + | <scene name='User:Vincent_de_Chavez/Sandbox_1/Testtowork/1'>TextToBeDisplayed</scene> | ||
Revision as of 05:00, 9 March 2009
|
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.
