Sandbox Reserved 801
From Proteopedia
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| - | <scene name='56/563213/Full_protein/2'>Succinyl-CoA synthetase</scene> is an enzyme that plays a key role in the citric acid cycle by catalyzing the reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP. The isoform shown here is from ''Sus scrofa'' and utilizes GTP. Other isoforms utilize ATP. Succinyl-CoA synthetase is a dimer composed of two chains, alpha and beta. The alpha chain is shown in green and the beta chain is shown in blue. The <scene name='56/563213/secondary_structure/1'>Secondary Structure</scene> is composed of alpha helices (blue), beta sheets (yellow), and nonrepetitive sequences. <scene name='56/563213/Hydrogen_bonding/3'>Hydrogen bonding</scene> stabilizes the structure of the protein and is evident especially in the alpha helices and beta sheets. The hydrogen bonds, shown in black, run down the length of the helices and between the strands of the beta sheets. There are relatively more hydrogen bonds between the sidechains on the exterior portion of the protein than the interior. This is largely a result of more hydrophobic <scene name='56/563213/side_chains/1'>Side Chains</scene> occuring in the interior and more hydrophilic residues occuring on the exterior, where they can interact with water. | + | <scene name='56/563213/Full_protein/2'>Succinyl-CoA synthetase</scene> is an enzyme that plays a key role in the citric acid cycle by catalyzing the reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP. The isoform shown here is from ''Sus scrofa'' and utilizes GTP. Other isoforms utilize ATP. Succinyl-CoA synthetase is a dimer composed of two chains, alpha and beta. The alpha chain is shown in green and the beta chain is shown in blue. The <scene name='56/563213/secondary_structure/1'>Secondary Structure</scene> is composed of alpha helices (blue), beta sheets (yellow), and nonrepetitive sequences. <scene name='56/563213/Hydrogen_bonding/3'>Hydrogen bonding</scene> stabilizes the structure of the protein and is evident especially in the alpha helices and beta sheets. The hydrogen bonds, shown in black, run down the length of the helices and between the strands of the beta sheets. There are relatively more hydrogen bonds between the sidechains on the exterior portion of the protein than the interior. This is largely a result of more hydrophobic <scene name='56/563213/side_chains/1'>Side Chains</scene> occuring in the interior and more hydrophilic residues occuring on the exterior, where they can interact with water. <scene name='56/563213/Solvent_interaction/1'>Solvent accessibility</scene> is highest on the outside of the protein and the region between the two subunits. |
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| - | <scene name='56/563213/Solvent_interaction/1'>Solvent accessibility</scene> | + | |
<scene name='56/563213/Ligand_binding/2'>Ligand Binding</scene> | <scene name='56/563213/Ligand_binding/2'>Ligand Binding</scene> | ||
<scene name='56/563213/Catalytic_residues/1'>Catalytic Residues</scene> | <scene name='56/563213/Catalytic_residues/1'>Catalytic Residues</scene> | ||
Revision as of 19:36, 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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Succinyl-CoA synthetase
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is an enzyme that plays a key role in the citric acid cycle by catalyzing the reaction of succinyl-CoA + NDP + Pi <-> succinate + CoA + NTP. The isoform shown here is from Sus scrofa and utilizes GTP. Other isoforms utilize ATP. Succinyl-CoA synthetase is a dimer composed of two chains, alpha and beta. The alpha chain is shown in green and the beta chain is shown in blue. The is composed of alpha helices (blue), beta sheets (yellow), and nonrepetitive sequences. stabilizes the structure of the protein and is evident especially in the alpha helices and beta sheets. The hydrogen bonds, shown in black, run down the length of the helices and between the strands of the beta sheets. There are relatively more hydrogen bonds between the sidechains on the exterior portion of the protein than the interior. This is largely a result of more hydrophobic occuring in the interior and more hydrophilic residues occuring on the exterior, where they can interact with water. is highest on the outside of the protein and the region between the two subunits.
