Sandbox 49

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. spinqualitylabelsall models <scene name= Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Introduction Lipase is an enzyme that functions to convert triacylglycerols to 2-monoacylglycerols, it catalyzes the reaction to break down lipids into its subunits. Lipase has 449 amino acid resiudes, and 2 domains, the C Terminal Domains is smaller with 112 residues, and the N Terminal Domain consists of 337 residues. The secondary structural elements of Lipase, including the name='Sandbox_49/Beta_sheets_test_1/1'>Beta Sheets</scene> that make up 30 percent of the amino acid chain, and involving 139 residues as well as the Alpha Helices that make up 22 percent and 102 residues characterize the structure of the protein. References https://www.brenda-enzymes.org/php/result_flat.php4?ecno=3.1.1.3 https://enzyme.expasy.org/cgi-bin/enzyme/enzyme-search-ec https://www.pdb.org/pdb/explore/explore.do?structureId=1HPL Fundamentals of Biochemistry, Voet hydrophobic residues Lipase Active Sites Alpha Helices Beta Sheets Turns N Terminal Domains Ca Ligands C Terminal Domains Lipase Inhibitor Disulfide Bonds