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Sandbox Reserved 787

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Revision as of 19:24, 15 October 2013 by Student (Talk | contribs)
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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

Aconitase

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Aconitase is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process. This diagram shows theof Aconitase. The Helices are represented with blue and the sheets are represented with purple. are shown in yellow, we can see that there are a few anti-parallel beta-sheets at the pointed end of the protein and a majority of parallel beta sheets are found throughout the protein. The are shown in green. The are displayed in blue. We can see that the majority of the hydrophobic residues are present towards the center of the protein, the hydrophilic residues flank more so on the outer portion of the protein. The are shown as blue bubbles and are on the exterior and throughout the inside of the protein. The ligands are labeled in purple and we can see that the water molecules don't interact with the ligand complex in the middle of the protein as no water molecules are present around the ligands.

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