Sandbox 52
From Proteopedia
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==Introduction== | ==Introduction== | ||
| - | The <scene name='Sandbox_52/Adenylate_kinase_chain_a/1'>secondary structure</scene> in chain A of adenylate kinase shows multiple alpha helicies and beta sheets. These <scene name='Sandbox_52/Helicies_and_beta_sheets/1'>alpha helicies and beta sheets</scene> can be shown in different colors, with the alpha helicies shown in cyan and the beta sheets shown in red. The <scene name='Sandbox_52/Hydrogen_bonds_shown/1'>hydrogen bonds</scene> within the structure of the protein can also be displayed in green. These can be scene within the alpha helicies, helping maintain the structure of the helix, and are also between beta sheets. Most of the beta sheets are running parallel, as indicated by the crooked hydrogen bonds. This formation is less stable than the straight, parallel hydrogen bonding of the antiparallel sheets. | + | The <scene name='Sandbox_52/Adenylate_kinase_chain_a/1'>secondary structure</scene> in chain A of adenylate kinase shows multiple alpha helicies and beta sheets. These <scene name='Sandbox_52/Helicies_and_beta_sheets/1'>alpha helicies and beta sheets</scene> can be shown in different colors, with the alpha helicies shown in cyan and the beta sheets shown in red. The <scene name='Sandbox_52/Hydrogen_bonds_shown/1'>hydrogen bonds</scene> within the structure of the protein can also be displayed in green. These can be scene within the alpha helicies, helping maintain the structure of the helix, and are also between beta sheets. Most of the beta sheets are running parallel, as indicated by the crooked hydrogen bonds. They are crooked due to the position of the carbonyl oxygens and amide hydrogens in the structure. This formation is less stable than the straight, parallel hydrogen bonding of the antiparallel sheets. The <scene name='Sandbox_52/Hydrophobic_residues/1'>hydrophobic residues</scene> on the structure can be seen in yellow sticks. Generally, these residues are clustered in the center of the protein due to the hydrophobic effect. |
Revision as of 19:32, 18 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. |
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Introduction
The in chain A of adenylate kinase shows multiple alpha helicies and beta sheets. These can be shown in different colors, with the alpha helicies shown in cyan and the beta sheets shown in red. The within the structure of the protein can also be displayed in green. These can be scene within the alpha helicies, helping maintain the structure of the helix, and are also between beta sheets. Most of the beta sheets are running parallel, as indicated by the crooked hydrogen bonds. They are crooked due to the position of the carbonyl oxygens and amide hydrogens in the structure. This formation is less stable than the straight, parallel hydrogen bonding of the antiparallel sheets. The on the structure can be seen in yellow sticks. Generally, these residues are clustered in the center of the protein due to the hydrophobic effect.
