Sandbox Reserved 789
From Proteopedia
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<Structure load='1CSC' size='500' frame='true' align='right' caption='Citrate Synthase' scene='Insert optional scene name here' /> | <Structure load='1CSC' size='500' frame='true' align='right' caption='Citrate Synthase' scene='Insert optional scene name here' /> | ||
Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a <scene name='56/563201/Homodimer/1'>homodimer</scene> of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes <scene name='56/563201/Secondary_structure/3'>secondary structure</scene>, with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue. | Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a <scene name='56/563201/Homodimer/1'>homodimer</scene> of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes <scene name='56/563201/Secondary_structure/3'>secondary structure</scene>, with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue. | ||
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| + | Here <scene name='56/563201/Hydrogen_bonds/1'>the hydrogen bonds</scene> in the backbone are depicted. Hydrogen bonding is what holds the molecule together, most notably the secondary structure. | ||
Here the <scene name='56/563201/Hydrophobic_residues/1'>hydrophobic residues</scene> are depicted, as well as the <scene name='56/563201/Hydrophilic_residues/1'>hydrophilic residues</scene>. | Here the <scene name='56/563201/Hydrophobic_residues/1'>hydrophobic residues</scene> are depicted, as well as the <scene name='56/563201/Hydrophilic_residues/1'>hydrophilic residues</scene>. | ||
<scene name='56/563201/Water_interactions/1'>Water molecules are</scene> represented by the blue spheres. A ligand is represented in purple. | <scene name='56/563201/Water_interactions/1'>Water molecules are</scene> represented by the blue spheres. A ligand is represented in purple. | ||
<scene name='56/563201/Ligand_interactions/1'>Ligand interactions</scene> are depicted in ball and stick and the rest of the protein is in ribbon. | <scene name='56/563201/Ligand_interactions/1'>Ligand interactions</scene> are depicted in ball and stick and the rest of the protein is in ribbon. | ||
<scene name='56/563201/Catalytic_residues/1'>Catalytic residues</scene> are shown in black. | <scene name='56/563201/Catalytic_residues/1'>Catalytic residues</scene> are shown in black. | ||
Revision as of 00:44, 17 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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Citrate synthase exists in nearly all cells, and is responsible for catalyzing the first reaction in the citric acid cycle: the condensation of acetyl-CoA and oxaloacetate to form citrate. Citrate synthase consists of 437 amino acids, which are organized in to two identical subunits. Citrate synthase is considered a of a single amino acid chain monomer, this makes up its tertiary structure. Each subunit consists of 20 alpha-helicies. Alpha-helicies make up the majority of the enzymes , with few beta sheets. The a- helicies are represented in purple, while the B- sheets are in blue.
Here in the backbone are depicted. Hydrogen bonding is what holds the molecule together, most notably the secondary structure. Here the are depicted, as well as the . represented by the blue spheres. A ligand is represented in purple. are depicted in ball and stick and the rest of the protein is in ribbon. are shown in black.
