Sandbox SouthUniversity1: Difference between revisions

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The reason that this flavone is bound so tightly to the enzyme is that it's shape and electronic charge are complementary to the binding pocket. This is examined <scene name='Sandbox_SouthUniversity1/2hi4_blue_transparent_ribbons/1'>next.</scene>  
The reason that this flavone is bound so tightly to the enzyme is that it's shape and electronic charge are complementary to the binding pocket. This is examined <scene name='Sandbox_SouthUniversity1/2hi4_blue_transparent_ribbons/1'>next.</scene>  


First examine the shape of the VDW area <scene name='Sandbox_SouthUniversity1/2hi4_bl_transp_rib_flav_vdw/1'>around the flavone.</scene>
First examine the shape of the VDW area <scene name='Sandbox_SouthUniversity1/2hi4_bl_transp_rib_flav_vdw/1'>around the flavone.</scene> The reddish areas show places where there are particularly close contacts with the binding pocket. These contacts can be caused by ionic, hydrophobic, or hydrogen bonding. Now we will examine what exactly is responsible for the tight binding.
 
Lets remove the rest of the protein, so we can better see these interactions.


First examine the shape of the <scene name='Sandbox_SouthUniversity1/2hi4_bl_transp_ribbon_flav_spc/1'>flavone </scene>bound to the protein.  
First examine the shape of the <scene name='Sandbox_SouthUniversity1/2hi4_bl_transp_ribbon_flav_spc/1'>flavone </scene>bound to the protein.  

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Arthur Cox