Sandbox Reserved 802
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| - | <Structure load=' | + | <Structure load='3dfo' size='500' frame='true' align='right' caption='Aldolase' scene='Insert optional scene name here' /> |
| - | The <scene name='56/563214/ | + | The <scene name='56/563214/Aldolase/1'>tertiary structure</scene> of Fructose Biphosphate Aldolase can be observed. Aldolase is an enzyme that is active during glycolysis in order to produce 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 sheet (<scene name='56/563214/A2_-_helices_and_sheets/1'>secondary structure</scene>). 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. |
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Revision as of 17:42, 12 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. |
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The of Fructose Biphosphate Aldolase can be observed. Aldolase is an enzyme that is active during glycolysis in order to produce 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 sheet (). 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.
