Sandbox 30

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. Trypsin spinqualitylabelsall models Click on the links to the left to view different structural aspects Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Overview and Function An easy way to distinguish between main structural component of the protein is to view it using rainbow coloration. To see various other specific structures of Trypsin, click on their links. Rainbow Coloration Skeletal Structure α Helices β Sheets Backbone Side Chains (orange) Polar (blue), and Nonpolar (Crimson) Water (blue) around Trypsin (orange) Hydrophobic Portion of Trypsin (red) Surface Structure Trypsin's primary amino acid sequence forms two α helices and two β sheets. Both of the α helices are right handed and the β sheets are anti-parallel. The order of the secondary structures is easily visible when using the rainbow coloration scheme to identify secondary structures. The N-terminus (blue) is the beginning of trypsin and the C-terminus (agua-green) is the end. Polar and Nonpolar Residues Ligand Interactions spinqualitylabelsall models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D