Sandbox 48: Difference between revisions
From Proteopedia
Jump to navigationJump to search
| Line 5: | Line 5: | ||
== Secondary Structure in Chain A == | == Secondary Structure in Chain A == | ||
We will be examining the structure of <scene name='Sandbox_48/Adenylate_kinase__chain_a/1'>chain A in | We will be examining the 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 Chain A of adenylate kinase includes alpha-helices (green), and beta-sheets (blue). The location of the <scene name='Sandbox_48/2_structure_hbondson/1'>hydrogen bonds</scene> within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. | 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). The location of the <scene name='Sandbox_48/2_structure_hbondson/1'>hydrogen bonds</scene> 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 (charged | 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. | ||
== Solvent Accessibility == | == Solvent Accessibility == | ||