Sandbox Reserved 788

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<Structure load='3IE7' size='500' frame='true' align='right' caption='Phosphofructokinase' scene='Insert optional scene name here' />
<Structure load='3IE7' size='500' frame='true' align='right' caption='Phosphofructokinase' scene='Insert optional scene name here' />
This is the <scene name='56/563200/Phosphofructokinase/1'>secondary structure</scene> of Phosphofructokinase.
This is the <scene name='56/563200/Phosphofructokinase/1'>secondary structure</scene> of Phosphofructokinase.
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It contains 10 <scene name='56/563200/Highlighted_alpha_and_beta/2'>α-helices and 14 β-sheets</scene>. The pattern of <scene name='56/563200/H-bonds/2'>backbone hydrogen bonding</scene> shows there to be a mixture of parallel and anti-parallel β-sheets. The parallel sheets can be identified by the angled hydrogen bonds, while the anti-parallel sheets contain straight hydrogen bonds. The hydrophobic (orange) and hydrophilic (blue) side chains <scene name='56/563200/Hydrophobic_and_hydrophilic/3'>side chains</scene>
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It contains 10 <scene name='56/563200/Highlighted_alpha_and_beta/3'>α-helices and 14 β-sheets</scene>. The pattern of <scene name='56/563200/H-bonds/2'>backbone hydrogen bonding</scene> shows there to be a mixture of parallel and anti-parallel β-sheets. The parallel sheets can be identified by the angled hydrogen bonds, while the anti-parallel sheets contain straight hydrogen bonds. A display of the hydrophobic (orange) and hydrophilic (blue) <scene name='56/563200/Hydrophobic_and_hydrophilic/4'>side chains</scene> shows that the hydrophobic groups are predominantly in the center of the protein, while the hydrophilic groups occupy the periphery and the active site. <scene name='56/563200/Water_localization/1'>Water molecules</scene> associate with the surface and active site of the enzyme. The position of the water molecules correspond with the of the hydrophilic side chains <scene name='56/563200/Side_chain_sticks_with_water/1'>locations</scene>, which is to be expected.
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Showing where waters are <scene name='56/563200/Water_localization/1'>TextToBeDisplayed</scene>
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<scene name='56/563200/Ligand_binding/1'>TextToBeDisplayed</scene>
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<scene name='56/563200/Ligand_binding/1'>TextToBeDisplayed</scene>
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<scene name='56/563200/Active_site/1'>TextToBeDisplayed</scene>
<scene name='56/563200/Active_site/1'>TextToBeDisplayed</scene>
<scene name='56/563200/Spacefilling/1'>TextToBeDisplayed</scene>
<scene name='56/563200/Spacefilling/1'>TextToBeDisplayed</scene>
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side chains with water

Revision as of 15:30, 10 October 2013

This Sandbox is Reserved from Oct 10, 2013, through May 20, 2014 for use in the course "CHEM 410 Biochemistry 1 and 2" taught by Hanna Tims at the Messiah College. This reservation includes Sandbox Reserved 780 through Sandbox Reserved 807.
To get started:
  • Click the edit this page tab at the top. Save the page after each step, then edit it again.
  • Click the 3D button (when editing, above the wikitext box) to insert Jmol.
  • show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page.
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More help: Help:Editing

Phosphofructokinase

Drag the structure with the mouse to rotate

This is the of Phosphofructokinase. It contains 10 . The pattern of shows there to be a mixture of parallel and anti-parallel β-sheets. The parallel sheets can be identified by the angled hydrogen bonds, while the anti-parallel sheets contain straight hydrogen bonds. A display of the hydrophobic (orange) and hydrophilic (blue) shows that the hydrophobic groups are predominantly in the center of the protein, while the hydrophilic groups occupy the periphery and the active site. associate with the surface and active site of the enzyme. The position of the water molecules correspond with the of the hydrophilic side chains , which is to be expected. side chains with water

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