Sandbox 52: Difference between revisions
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==Introduction== | ==Introduction== | ||
Adenylate kinase is an enzyme that catalyzes the following reaction: ATP+ AMP <-> ADP + ADP. This is a very useful reaction in the body, since it allows the body to maintain homeostasis in levels of ATP, an energy source in the body. Its unique structure allows it to bind the substrates or other non-hydrolysable ligands. The <scene name='Sandbox_52/Adenylate_kinase_chain_a/1'>secondary structure</scene> in chain A of adenylate kinase shows multiple <scene name='Sandbox_52/Helicies_and_beta_sheets/1'>alpha helicies(cyan) and beta sheets(red)</scene>. ==Hydrogen Bonding== | Adenylate kinase is an enzyme that catalyzes the following reaction: ATP+ AMP <-> ADP + ADP. This is a very useful reaction in the body, since it allows the body to maintain homeostasis in levels of ATP, an energy source in the body. Its unique structure allows it to bind the substrates or other non-hydrolysable ligands. The <scene name='Sandbox_52/Adenylate_kinase_chain_a/1'>secondary structure</scene> in chain A of adenylate kinase shows multiple <scene name='Sandbox_52/Helicies_and_beta_sheets/1'>alpha helicies(cyan) and beta sheets(red)</scene>. | ||
==Hydrogen Bonding== | |||
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 seen 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/Hydrogen_bonds_shown/1'>hydrogen bonds</scene> within the structure of the protein can also be displayed in green. These can be seen 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. | ||
==Hydrophobic and Hydrophilic Interactions== | ==Hydrophobic and Hydrophilic Interactions== | ||
