Sandbox 37: Difference between revisions
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<Structure load='1AKE' size='500' frame='true' align='right' caption='Adenylate Kinase' scene='Matt's Beautiful Protein' /> | |||
The <scene name='Sandbox_37/Matt_adenylate_kinase_37/1'>Adenylate Kinase</scene> protein is shown here with alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). | |||
The <scene name='Sandbox_37/Matt_helix_beta_colored/1'>Secondary Structure</scene> of the protein is shown here with alpha helices (green) and beta sheets (blue) highlighted appropriately. | |||
The <scene name='Sandbox_37/Matt_hydrogen_bonds_good/1'>Hydrogen Bonds</scene> of chain A of the protein are highlighted in orange here. | |||
The <scene name='Sandbox_37/Matt_hydrophobic_good/1'>Hydrophobic Interactions</scene> are shown here in red. | |||
The <scene name='Sandbox_37/Matt_hydrophilic_good/1'>Hydrophilic Interactions</scene> are shown here in black. | |||
The <scene name='Sandbox_37/Matt_solvent/1'>Solvent</scene> , which is water, is shown here in red. Water's primary location is on the outer parts of the protein, or the hydrophilic regions. | |||
The side chains that interact with the <scene name='Sandbox_37/Matt_ligand/1'>ligand</scene> are shown here in crimson. The interactions occur with the hydrophobic side chains. The rest of the protein is faded blue. | |||
The <scene name='Sandbox_37/Matt_catalytic_residues/1'>catalytic residues</scene> of this protein are shown here in lime green. | |||
Latest revision as of 02:21, 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.
The Adenylate Kinase protein is shown here with alpha helices (cyan) and beta sheets (green) surrounding the non-hydrolysable substrate analogue (orange). The Secondary Structure of the protein is shown here with alpha helices (green) and beta sheets (blue) highlighted appropriately. The Hydrogen Bonds of chain A of the protein are highlighted in orange here. The Hydrophobic Interactions are shown here in red. The Hydrophilic Interactions are shown here in black. The Solvent , which is water, is shown here in red. Water's primary location is on the outer parts of the protein, or the hydrophilic regions. The side chains that interact with the ligand are shown here in crimson. The interactions occur with the hydrophobic side chains. The rest of the protein is faded blue. The catalytic residues of this protein are shown here in lime green. |