Sandbox Reserved 799
From Proteopedia
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<Structure load='2H88' size='500' frame='true' align='right' caption='Succinate dehydrogenase' scene='Insert optional scene name here' /> | <Structure load='2H88' size='500' frame='true' align='right' caption='Succinate dehydrogenase' scene='Insert optional scene name here' /> | ||
Succinate dehydrogenase is an important enzyme in the citric acid cycle that converts succinate to fumarate, two intermediate carbon compounds in the cycle. Succinate dehydrogenase is an integrated membrane protein that exists in the inner membrane of the mitochondria. This diagram shows two enzymes in a complex working together from ''Gallus gallus'', the common chicken. The individual enzyme exists as a <scene name='56/563211/Tetramer/1'>tetramer</scene>. | Succinate dehydrogenase is an important enzyme in the citric acid cycle that converts succinate to fumarate, two intermediate carbon compounds in the cycle. Succinate dehydrogenase is an integrated membrane protein that exists in the inner membrane of the mitochondria. This diagram shows two enzymes in a complex working together from ''Gallus gallus'', the common chicken. The individual enzyme exists as a <scene name='56/563211/Tetramer/1'>tetramer</scene>. | ||
| - | The <scene name='56/563211/Secondary_structure/2'>secondary structure</scene> of the enzyme is primarily alpha helices, illustrated in red, and beta sheets, illustrated in blue. There is also non-repetitive coil, seen in white. <scene name='56/563211/Black_bonds_of_hydrogen/1'>Hydrogen bonds</scene> of the backbone are visible in black. The pattern of hydrogen bonding on the beta sheets indicates that they are anti-parallel. This enzyme contains no sulfide bonds responsible for stabilizing tertiary structure. The <scene name='56/563211/Hydrophobic_and_hydrophilic/1'>hydrophobic and hydrophilic residues</scene> for succinate dehydrogenase are illustrated here; grey represents the hydrophobic side chain residues, and orange represents charged and hydrophilic side chain residues. This transmembrane enzyme has contact with the <scene name='56/563211/Solvent/1'>water solvent</scene> at the end of the protein that exists outside the membrane. In this figure, water molecules are illustrated in dark blue. The <scene name='56/563211/Solvent_and_ligand/2'>ligands</scene>, seen in pink, interact at multiple points on the enzyme. The enzyme has <scene name='56/563211/Interacts_with_things/1'>contacts with the ligand</scene> | + | The <scene name='56/563211/Secondary_structure/2'>secondary structure</scene> of the enzyme is primarily alpha helices, illustrated in red, and beta sheets, illustrated in blue. There is also non-repetitive coil, seen in white. <scene name='56/563211/Black_bonds_of_hydrogen/1'>Hydrogen bonds</scene> of the backbone are visible in black. The pattern of hydrogen bonding on the beta sheets indicates that they are anti-parallel. This enzyme contains no sulfide bonds responsible for stabilizing tertiary structure. The <scene name='56/563211/Hydrophobic_and_hydrophilic/1'>hydrophobic and hydrophilic residues</scene> for succinate dehydrogenase are illustrated here; grey represents the hydrophobic side chain residues, and orange represents charged and hydrophilic side chain residues. This transmembrane enzyme has contact with the <scene name='56/563211/Solvent/1'>water solvent</scene> at the end of the protein that exists outside the membrane. In this figure, water molecules are illustrated in dark blue. The <scene name='56/563211/Solvent_and_ligand/2'>ligands</scene>, seen in pink, interact at multiple points on the enzyme. The enzyme has <scene name='56/563211/Interacts_with_things/1'>contacts with the ligand</scene> at various side chain residues, represented in dark blue. These residues of contact are polar or charged, and this helps to stabilize the oxygenated ligand, succinate, for its catalysis. |
Revision as of 20:14, 16 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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Succinate dehydrogenase is an important enzyme in the citric acid cycle that converts succinate to fumarate, two intermediate carbon compounds in the cycle. Succinate dehydrogenase is an integrated membrane protein that exists in the inner membrane of the mitochondria. This diagram shows two enzymes in a complex working together from Gallus gallus, the common chicken. The individual enzyme exists as a . The of the enzyme is primarily alpha helices, illustrated in red, and beta sheets, illustrated in blue. There is also non-repetitive coil, seen in white. of the backbone are visible in black. The pattern of hydrogen bonding on the beta sheets indicates that they are anti-parallel. This enzyme contains no sulfide bonds responsible for stabilizing tertiary structure. The for succinate dehydrogenase are illustrated here; grey represents the hydrophobic side chain residues, and orange represents charged and hydrophilic side chain residues. This transmembrane enzyme has contact with the at the end of the protein that exists outside the membrane. In this figure, water molecules are illustrated in dark blue. The , seen in pink, interact at multiple points on the enzyme. The enzyme has at various side chain residues, represented in dark blue. These residues of contact are polar or charged, and this helps to stabilize the oxygenated ligand, succinate, for its catalysis.
