Sandbox Reserved 782

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As previously mentioned, the hydrophobic interactions are critical in determining the protein structure. Here, the <scene name='56/563194/Solvent/1'>interactions with water</scene> show that the water molecules predominantly gather around the outside of the protein, which is where most of the hydrophilic residues lie.
As previously mentioned, the hydrophobic interactions are critical in determining the protein structure. Here, the <scene name='56/563194/Solvent/1'>interactions with water</scene> show that the water molecules predominantly gather around the outside of the protein, which is where most of the hydrophilic residues lie.
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<scene name='56/563194/Interactions/1'>interactions with ligands</scene>
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<scene name='56/563194/Interactions/1'>interactions with ligands</scene>
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 +
Or alternate interactions showing the ATP molecule in green, with the ligands in yellow? <scene name='56/563194/Alternate_interactions/1'>Alternate interaction</scene>
==Active Site==
==Active Site==
The active site is made up of <scene name='56/563194/Interactions_with_catalyst/1'>catalytic residues</scene>
The active site is made up of <scene name='56/563194/Interactions_with_catalyst/1'>catalytic residues</scene>

Revision as of 18:26, 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.
  • Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc.

More help: Help:Editing

Phosphofructokinase from Listeria

Drag the structure with the mouse to rotate

Phosphofructokinase

This is the of Phosphofructokinase. The Purple designates the alpha helices...finish description

The bulk of this proteins structure is made up of the alpha helices are in yellow and the beta sheets are in grey. In addition the three green balls represent the three Mg atoms, the internal compound is ATP and the small grey and red group off to the side is the glycerol.

is a very important part of protein structure shape and stability. The hydrogen bonds of phosphofructokinase are designated by the orange dotted lines throughout the structure. Phosphofructokinase contains both anti-parallel and parallel sheets, which are identified by parallel hydrogen bonds and angled hydrogen bonds respectively.

One of the most important determining factors of protein structure lies in hydrophobic interactions between the with the surrounding environment. The hydrophobic residues are designated with light green while the hydrophobic residues are shown in blue. As would be expected the majority of the hydrophobic residues are located at the center of the protein where they are shielded from the hydrophobic environment.

As previously mentioned, the hydrophobic interactions are critical in determining the protein structure. Here, the show that the water molecules predominantly gather around the outside of the protein, which is where most of the hydrophilic residues lie.

Or alternate interactions showing the ATP molecule in green, with the ligands in yellow?

Active Site

The active site is made up of

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