From Proteopedia
proteopedia linkproteopedia link
| 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
|
Introduction and structure
can be observed. Aldolase is an enzyme that is active during glycolysis, which is an overall series of reactions that produces cellular energy (ATP). Specifically, aldolase catalyzes an aldol cleavage reaction that hydrolyzes fructose 1,6-bisphosphate. It is a tetrameter (four subunits)composed of alpha helices and beta sheets (). Please note that alpha helices are observed in blue, and beta sheets are in yellow. The majority of the helices are located on the surface (outside) of the enzyme, where as most of the sheets are found in the interior. Most likely, polar amino acids are located on the peripheral helices, while hydrophobic or paired-polar amino acids are found within the beta sheet.
