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Sandbox Reserved 787
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This diagram shows the<scene name='56/563199/Aconitase_secondary_structure/1'>Secondary structure</scene>of Aconitase. The Helices are represented with blue and the sheets are represented with purple. | This diagram shows the<scene name='56/563199/Aconitase_secondary_structure/1'>Secondary structure</scene>of Aconitase. The Helices are represented with blue and the sheets are represented with purple. | ||
<scene name='56/563199/Aconitase_hydrogen_bonds/1'>Hydrogen Bonds</scene> are shown in yellow, we can see that there are a few anti-parallel beta-sheets at the pointed end of the protein and a majority of parallel beta sheets are found throughout the protein. | <scene name='56/563199/Aconitase_hydrogen_bonds/1'>Hydrogen Bonds</scene> are shown in yellow, we can see that there are a few anti-parallel beta-sheets at the pointed end of the protein and a majority of parallel beta sheets are found throughout the protein. | ||
| - | The <scene name='56/563199/ | + | The <scene name='56/563199/Hydrophobic_residues/1'>Hydrophobic residues</scene> are shown in green. |
| + | The <scene name='56/563199/Hydrophilic_residues/1'>Hydrophilic residues</scene> are displayed in blue. | ||
Revision as of 18:42, 15 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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Aconitase is an enzyme that catalyses the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process. This diagram shows theof Aconitase. The Helices are represented with blue and the sheets are represented with purple. are shown in yellow, we can see that there are a few anti-parallel beta-sheets at the pointed end of the protein and a majority of parallel beta sheets are found throughout the protein. The are shown in green. The are displayed in blue.
