Sandbox Reserved 786

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The <scene name='56/563198/Unedited/1'>crystaline structure of malate dehydrogenase</scene> shows that it is a homo-tetramer. However the <scene name='56/563198/Green_helices_red_beta-sheets/2'>biological unit</scene> is a dimer. In the image, the alpha-helices are green, Beta-sheets are red, and random coils (turns) are grey.
The <scene name='56/563198/Unedited/1'>crystaline structure of malate dehydrogenase</scene> shows that it is a homo-tetramer. However the <scene name='56/563198/Green_helices_red_beta-sheets/2'>biological unit</scene> is a dimer. In the image, the alpha-helices are green, Beta-sheets are red, and random coils (turns) are grey.
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== '''Secondary Structure''' ==
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The <scene name='56/563198/Greenred-whbond/1'>secondary structure of malate dehydrogenase</scene> is formed by hydrogen bonding interactions of the amino acids backbone. There are two beta-sheet regions in each monomer of the natural dimer. Five beta-sheets in each monomer are anti-parallel, and form a pseudo beta-barrel motif. Six beta-sheets in each monomer show parallel configuration. The angle of the hydrogen bonds relative to one another between beta-sheets gives insight as to which beta-sheets are parallel and which are anti-parallel. Parallel beta-sheets have "crooked" h-bonding. This makes them more unstable than the anti-parallel beta-sheets

Revision as of 15:44, 20 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

Malate Dehydrogenase

Drag the structure with the mouse to rotate

The shows that it is a homo-tetramer. However the is a dimer. In the image, the alpha-helices are green, Beta-sheets are red, and random coils (turns) are grey.


Secondary Structure

The is formed by hydrogen bonding interactions of the amino acids backbone. There are two beta-sheet regions in each monomer of the natural dimer. Five beta-sheets in each monomer are anti-parallel, and form a pseudo beta-barrel motif. Six beta-sheets in each monomer show parallel configuration. The angle of the hydrogen bonds relative to one another between beta-sheets gives insight as to which beta-sheets are parallel and which are anti-parallel. Parallel beta-sheets have "crooked" h-bonding. This makes them more unstable than the anti-parallel beta-sheets

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