Sandbox 42: Difference between revisions
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<scene name='Sandbox_42/Wes_-_hydrophobic_residues/1'>hydrophobic residues</scene> in gray | <scene name='Sandbox_42/Wes_-_hydrophobic_residues/1'>hydrophobic residues</scene> in gray | ||
<scene name='Sandbox_42/Wes_-_polar-charged_residues/1'>polar and charged residues</scene> in brown | <scene name='Sandbox_42/Wes_-_polar-charged_residues/1'>polar and charged residues</scene> in brown | ||
<scene name='Sandbox_42/Wes_-_water-secondary_update/ | <scene name='Sandbox_42/Wes_-_water-secondary_update/2'>Water</scene> in yellow - secondary structure | ||
<scene name='Sandbox_42/Wes_-_water-ball_and_stick/1'>Water</scene> in yellow - ball/stick | <scene name='Sandbox_42/Wes_-_water-ball_and_stick/1'>Water</scene> in yellow - ball/stick | ||
<scene name='Sandbox_42/Wes_-_ligand/1'>ligand</scene> and interacting side chains are shown here in stick/wire representation, with the rest of the protein semi-transparent. | |||
Revision as of 21:24, 14 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.
IntroductionAdenylate kinase consists of two chains, Chain A and Chain B. The secondary structure is highlighted here, with alpha helices (shown in green) and beta sheets (blue). Hydrogen bonds are shown in black. These bonds show that the beta sheets are connected in parallel, as the hydrogen bonds are angled and not parallel to one another. hydrophobic residues in gray polar and charged residues in brown Water in yellow - secondary structure Water in yellow - ball/stick ligand and interacting side chains are shown here in stick/wire representation, with the rest of the protein semi-transparent. |
