Sandbox 48: Difference between revisions
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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 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/ | 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 are located closest on the inside of the enzyme. The <scene name='Sandbox_48/Secondary__structure__hydrophi/1'>hydrophillic residues</scene> (charged and polar) are on the outward face of the enzyme. | |||
Revision as of 19:39, 10 October 2012
Please do NOT make changes to this Sandbox. Sandboxes 30-60 are reserved for use by Biochemistry 410 & 412 at Messiah College taught by Dr. Hannah Tims during Fall 2012 and Spring 2013.
Secondary Structure in Chain AWe will be examining the structure of chain A in Adenylate Kinase The secondary structures of Chain A of adenylate kinase includes alpha-helices (green), and beta-sheets (blue). The location of the hydrogen bonds within the secondary structure demonstrates how the alpha-helices and beta-sheets are hydrogen bonded. Within these structures the hydrophobic residues are located closest on the inside of the enzyme. The hydrophillic residues (charged and polar) are on the outward face of the enzyme. |
