Sandbox 44
From Proteopedia
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The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. | The <scene name='Sandbox_44/Secondary_structures/1'>Secondary Structure</scene> of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. | ||
The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). | The <scene name='Sandbox_44/Hydrogen_bonds/1'>Hydrogen Bonds</scene> of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). | ||
| - | The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site. | + | The enzyme has <scene name='Sandbox_44/Hydrophobic_residues/2'>Hydrophobic Residues</scene> (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has <scene name='Sandbox_44/Hydrophillic/1'>Hydrophillic</scene> residues (purple) located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site. |
The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly. | The <scene name='Sandbox_44/Ligand_interraction/1'>ligand</scene> in the center of the protein has <scene name='Sandbox_44/Catalytic_residues/1'>Catalytic Residues</scene> that allow binding to occur. The <scene name='Sandbox_44/Solvent/1'>water</scene> can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly. | ||
Revision as of 17:37, 19 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. |
Adenylate Kinase
Adenylate Kinase is an enzyme that helps in the conversion of 2 units of ADP into one of ATP and one of AMP. It has two chains:
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Structure
The of Adenylate Kinase consists of alpha helices (purple) and the beta sheets(lime green). There are seven sheets and 12 helices. The of the backbone are shown in yellow. They provide the structure by holding the protein together and giving it its shape.(Link may not show up). The enzyme has (blue)that are located are the inside of the protein. This makes sense because the enzyme is surrounded by water, and thus these residues would want to be as far away from this as possible. The enzyme also has residues (purple) located on the outside, which have an affinity for water and allow for the enzyme to move and function in the water and let substrate reach the active site. The in the center of the protein has that allow binding to occur. The can't interract with the ligand, because it is centrally located. This allows the active site not to be interfered with, and allows the enzyme to function properly.
Sources
http://en.wikipedia.org/wiki/Adenylate_kinase http://www.proteopedia.org/wiki/index.php/Adenylate_kinase
