Sandbox 48: Difference between revisions
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Adenylate kinase (or ADK) is an enzyme known to catalyze the interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP), and vice versa. This enzyme is imporant for cellular energy homeostasis because the need for ADP. ADP is required for oxidative phosphorylation, an important step in multiple metabolic pathways. | Adenylate kinase (or ADK) is an enzyme known to catalyze the interconversion of adenosine triphosphate (ATP) and adenosine monophosphate (AMP) to two molecules of adenosine diphosphate (ADP), and vice versa. This enzyme is imporant for cellular energy homeostasis because the need for ADP. ADP is required for oxidative phosphorylation, an important step in multiple metabolic pathways. | ||
== Secondary Structure | == Secondary Structure == | ||
We will be examining the structure of <scene name='Sandbox_48/Adenylate_kinase__chain_a/1'>chain A in adenylate kinase</scene>. | We will be examining the secondary structure of <scene name='Sandbox_48/Adenylate_kinase__chain_a/1'>chain A in adenylate kinase</scene>. | ||
The <scene name='Sandbox_48/Secondary__structure__greenblu/1'>secondary structures</scene> of | The <scene name='Sandbox_48/Secondary__structure__greenblu/1'>secondary structures</scene> of chain A of adenylate kinase includes alpha-helices (green), and beta-sheets (blue). There are 12 total helices in the enzyme, and 2 types of beta sheets, a parallel with 5 strands and an antiparallel with 2 strands. The location of the <scene name='Sandbox_48/2_structure_hbondson/1'>hydrogen bonds</scene> (black) within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. | ||
Within these structures the <scene name='Sandbox_48/Secondary__structure__hydropho/1'>hydrophobic</scene> residues (purple) are located closest on the inside of the enzyme. The <scene name='Sandbox_48/Secondary__structure__hydrophi/1'>hydrophillic </scene> residues (green), which are those that are charged or polar, are on the outward face of the enzyme. | Within these structures the <scene name='Sandbox_48/Secondary__structure__hydropho/1'>hydrophobic</scene> residues (purple) are located closest on the inside of the enzyme. The <scene name='Sandbox_48/Secondary__structure__hydrophi/1'>hydrophillic </scene> residues (green), which are those that are charged or polar, are on the outward face of the enzyme. | ||
