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Sandbox Reserved 787
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<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/Hydrophobic_residues/1'>Hydrophobic residues</scene> are shown in green. | 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. | + | The <scene name='56/563199/Hydrophilic_residues/1'>Hydrophilic residues</scene> are displayed in blue. We can see that the majority of the hydrophobic residues are present towards the center of the protein, the hydrophilic residues flank more so on the outer portion of the protein. |
Revision as of 18:45, 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. We can see that the majority of the hydrophobic residues are present towards the center of the protein, the hydrophilic residues flank more so on the outer portion of the protein.
