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Sandbox Reserved 783

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This image depicts the <scene name='56/563195/Fumarase-helicies_and_sheets/1'>secondary structure</scene> of fumarase. Alpha helicies are represented in coral color, and beta sheets are yellow. Alpha helicies make up most of the structure of fumarase. There are also random chains colored blue and green within this depiction of its secondary structure. The ligand is represented by red and gray molecules at the end of the alpha helicies.
This image depicts the <scene name='56/563195/Fumarase-helicies_and_sheets/1'>secondary structure</scene> of fumarase. Alpha helicies are represented in coral color, and beta sheets are yellow. Alpha helicies make up most of the structure of fumarase. There are also random chains colored blue and green within this depiction of its secondary structure. The ligand is represented by red and gray molecules at the end of the alpha helicies.
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Some of the <scene name='56/563195/Fumarase-hydrophobic3/1'>hydrophobic</scene> portions of fumarase (gray) and <scene name='56/563195/Fumarase-hydrophobicphilic2/1'>hydrophillic</scene> portions (yellow) illustrate the complexity of residue interactions with the solvent (water).
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Some of the <scene name='56/563195/Fumarase-hydrophobic3/1'>hydrophobic</scene> portions of fumarase (gray) and <scene name='56/563195/Fumarase-hydrophobicphilic2/1'>hydrophillic</scene> portions (red) illustrate the complex interactions between residues. It can also be observed that many hydrophobic portions are present...
<scene name='56/563195/Fumarasewater/2'>Solvent accessibility</scene> is shown through the blue spheres representing water and the white portion of fumarase itself. As can be seen, the center of the alpha helicies is inaccessible to solvent, as is certain portions of the motif near the catalitic residues.
<scene name='56/563195/Fumarasewater/2'>Solvent accessibility</scene> is shown through the blue spheres representing water and the white portion of fumarase itself. As can be seen, the center of the alpha helicies is inaccessible to solvent, as is certain portions of the motif near the catalitic residues.

Revision as of 04:51, 18 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

Fumarase

Drag the structure with the mouse to rotate

is awesome!!

Fumarase

This image depicts the of fumarase. Alpha helicies are represented in coral color, and beta sheets are yellow. Alpha helicies make up most of the structure of fumarase. There are also random chains colored blue and green within this depiction of its secondary structure. The ligand is represented by red and gray molecules at the end of the alpha helicies.

Some of the portions of fumarase (gray) and portions (red) illustrate the complex interactions between residues. It can also be observed that many hydrophobic portions are present... is shown through the blue spheres representing water and the white portion of fumarase itself. As can be seen, the center of the alpha helicies is inaccessible to solvent, as is certain portions of the motif near the catalitic residues.

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