Sandbox 40
From Proteopedia
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<StructureSection load='1hpl' size='500' side='right' caption='Structure of Horse Pancreatic Lipase (PDB entry [[1hpl]])' scene=''>Lipase, as its name suggests, is an enzyme responsible for the cleavage of types of lipid molecules. There are different types of lipases, many of which work in similar ways. For instance, Human Pancreatic Lipase, or HPL, splits triglycerides, the main lipids in the human diet, into glycerol and three fatty acids. The structure shown at right is that of Horse Pancreatic Lipase. It consists of two identical subunits, totaling 449 amino acids each. | <StructureSection load='1hpl' size='500' side='right' caption='Structure of Horse Pancreatic Lipase (PDB entry [[1hpl]])' scene=''>Lipase, as its name suggests, is an enzyme responsible for the cleavage of types of lipid molecules. There are different types of lipases, many of which work in similar ways. For instance, Human Pancreatic Lipase, or HPL, splits triglycerides, the main lipids in the human diet, into glycerol and three fatty acids. The structure shown at right is that of Horse Pancreatic Lipase. It consists of two identical subunits, totaling 449 amino acids each. | ||
The <scene name='Sandbox_40/Qm_lipase_secondary_structures/2'>secondary structures</scene> of lipase (just one subunit) include 102 residues which create 13 alpha helices, shown in red, and 139 residues involved in beta sheets totaling 28 strands, shown in gold. Lipase of course consists of both | The <scene name='Sandbox_40/Qm_lipase_secondary_structures/2'>secondary structures</scene> of lipase (just one subunit) include 102 residues which create 13 alpha helices, shown in red, and 139 residues involved in beta sheets totaling 28 strands, shown in gold. Lipase of course consists of both | ||
| - | <scene name='Sandbox_40/Lipase_qm/2'>polar and nonpolar residues</scene>. The polar residues in this scene are shown in a light blue shade, and the nonpolar are in a dark red. From this representation, it can be assumed that there is a similar quantity of polar residues as there are nonopolar. The tertiary stucture of the molecule is stabilized by 6 disulfide bonds and ionic interactions with a calcium ligand. Finally, the quaternary structure is completed by the adjoining of the two identical subunits. | + | <scene name='Sandbox_40/Lipase_qm/2'>polar and nonpolar residues</scene>. The polar residues in this scene are shown in a light blue shade, and the nonpolar are in a dark red. From this representation, it can be assumed that there is a similar quantity of polar residues as there are nonopolar. The tertiary stucture of the molecule is stabilized by 6 <scene name='Sandbox_40/Disulfide_bonds/1'>disulfide bonds</scene> and ionic interactions with a calcium ligand. Finally, the quaternary structure is completed by the adjoining of the two identical subunits. |
=The Calcium Ligand= | =The Calcium Ligand= | ||
<scene name='Sandbox_40/Lipase_ligand/1'>Lipase Ligand</scene> | <scene name='Sandbox_40/Lipase_ligand/1'>Lipase Ligand</scene> | ||
Revision as of 02:02, 14 November 2011
| 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. |
Horse Pancreatic Lipase
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