Sandbox Reserved 795
From Proteopedia
(Difference between revisions)
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- | <!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | + | <Structure load='Insert PDB code or filename here' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' /><!-- PLEASE DO NOT DELETE THIS TEMPLATE --> |
{{User:Hanna_Tims/Template_CHEM_410}} | {{User:Hanna_Tims/Template_CHEM_410}} | ||
<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | <!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
==Introduction and General Structure== | ==Introduction and General Structure== | ||
- | <Structure load=' | + | <Structure load='1u8f' size='500' frame='true' align='right' caption='Glyceraldehyde-3-phosphate dehydrogenase' scene='Insert optional scene name here' /> Glyceraldehyde 3-phosphate dehydrogenase, or G-3-P dehydrogenase, is an enzyme that plays a significant role in metabolism. It catalyzes a step in glycolysis in which glyceraldehyde 3-phosphate is converted to 3-phospho-D-glyceroyl phosphate. G-3-P dehydrogenase is a tetramer protein made up of four subunits. The <scene name='56/563207/Secondary_structure/1'>secondary structure</scene> of G-3-P dehydrogenase consists of alpha helices which are displayed in purple and beta sheets which are displayed in green. The beta sheets are parallel. |
==Hydrogen Bonds== | ==Hydrogen Bonds== | ||
The <scene name='56/563207/Hydrogen_bonding/2'>hydrogen bonding</scene> of the backbone is displayed in green. There are no disulfide bonds present in this enzyme. | The <scene name='56/563207/Hydrogen_bonding/2'>hydrogen bonding</scene> of the backbone is displayed in green. There are no disulfide bonds present in this enzyme. |
Revision as of 02:41, 15 October 2013
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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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Introduction and General Structure
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Hydrogen Bonds
The of the backbone is displayed in green. There are no disulfide bonds present in this enzyme.