Sandbox 250: Difference between revisions
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==='''Models of AChE'''=== | |||
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<applet load='2ace' size='300' frame='true' align='left' scene='Sandbox_250/Ache_ach/30' caption='AChE in complex with ACh'/> | <applet load='2ace' size='300' frame='true' align='left' scene='Sandbox_250/Ache_ach/30' caption='AChE in complex with ACh(2ace)'/> | ||
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<applet load='1fss' size='300' frame='true' align='left' scene='Sandbox_250/Ache_fas2/15' caption='AChE in complex with FAS-II'/> | <applet load='1fss' size='300' frame='true' align='left' scene='Sandbox_250/Ache_fas2/15' caption='AChE in complex with FAS-II(1fss)'/> | ||
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<scene name='Sandbox_250/Ache_ach/34'>CAS</scene>, highlighted in red, holds ACh in the optimal position for hydrolysis by interacting with the quaternary ammonium ion of ACh. | <scene name='Sandbox_250/Ache_ach/34'>CAS</scene>, highlighted in red, holds ACh in the optimal position for hydrolysis by interacting with the quaternary ammonium ion of ACh. | ||
The AChE active site includes three residues that form a catalytic triad: <scene name='Sandbox_250/Ache_ach/20'>Ser200, Glu327, and His440</scene>. The <scene name='Sandbox_250/Ache_ach/33'>Catalytic Triad</scene>, | The AChE active site includes three residues that form a catalytic triad: <scene name='Sandbox_250/Ache_ach/20'>Ser200, Glu327, and His440</scene>. The <scene name='Sandbox_250/Ache_ach/33'>Catalytic Triad</scene>, highlighted in blue, is responsible for the hydrolysis of ACh into acetate and choline. | ||
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A | A PowerPoint presentation of our project was given at the 2010 Rockefeller University NYC SMART Teams Annual Symposium. | ||
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