Sandbox Reserved 790

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<Structure load='4IP7' size='500' frame='true' align='right' caption='Pyruvate Kinase' scene='Insert optional scene name here' />
<Structure load='4IP7' size='500' frame='true' align='right' caption='Pyruvate Kinase' scene='Insert optional scene name here' />
The <scene name='56/563202/Colored_enzyme/1'>secondary structure</scene> of pyruvate kinase shows alpha helices (pink) surrounding beta sheets (blue) in a tetramer.
The <scene name='56/563202/Colored_enzyme/1'>secondary structure</scene> of pyruvate kinase shows alpha helices (pink) surrounding beta sheets (blue) in a tetramer.
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The <scene name='56/563202/Hydrophilic_residues/1'>hydrophilic and hydrophobic residues</scene> are shown here. The <scene name='56/563202/Hydrophilic_residues/2'>hydrophilic residues</scene> are shown in blue, and the <scene name='56/563202/Hydrophobic_esidues/1'>hydrophobic residues</scene> are shown in green.
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The <scene name='56/563202/Hydrophilic_residues/1'>hydrophilic and hydrophobic residues</scene> are shown here. The <scene name='56/563202/Hydrophilic_residues/2'>hydrophilic residues</scene> are highlighted in blue; these are found on the outer surface of the protein since they interact with the solvent. The <scene name='56/563202/Hydrophobic_esidues/1'>hydrophobic residues</scene> are highlighted in green and are found on the interior of the protein, away from the solvent.
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<scene name='56/563202/Water_and_non_water/1'>Water molecules</scene> are shown within the structure in green, and the non-water parts of the enzyme are shown in purple.
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<scene name='56/563202/Water_and_non_water/1'>Water molecules</scene> (the solvent with which the protein is interacting) are shown within the structure in green, and the non-water parts of the enzyme are shown in purple.
The <scene name='56/563202/Ligands/2'>ligand contact points</scene> in pyruvate kinase are highlighted in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine
The <scene name='56/563202/Ligands/2'>ligand contact points</scene> in pyruvate kinase are highlighted in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine

Revision as of 14:50, 17 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.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Pyruvate Kinase

Drag the structure with the mouse to rotate

The of pyruvate kinase shows alpha helices (pink) surrounding beta sheets (blue) in a tetramer. The are shown here. The are highlighted in blue; these are found on the outer surface of the protein since they interact with the solvent. The are highlighted in green and are found on the interior of the protein, away from the solvent. (the solvent with which the protein is interacting) are shown within the structure in green, and the non-water parts of the enzyme are shown in purple. The in pyruvate kinase are highlighted in green. The interacting groups are made up of charged residues like aspartate, glutamate, lysine, and histidine

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