Sandbox 40
From Proteopedia
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{{Template:Oberholser_Sandbox_Reservation}} | {{Template:Oberholser_Sandbox_Reservation}} | ||
Introduction <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 449 amino acids. | Introduction <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 449 amino acids. | ||
| - | <scene name='Sandbox_40/Qm_lipase_secondary_structures/1'> | + | The <scene name='Sandbox_40/Qm_lipase_secondary_structures/1'>secondary structures</scene> of lipase include 102 residues creating 13 alpha helices and 139 residues involved in beta sheets totaling 28 strands. |
<scene name='Sandbox_40/Lipase_qm/1'>Hydrophobic Residues</scene></StructureSection> | <scene name='Sandbox_40/Lipase_qm/1'>Hydrophobic Residues</scene></StructureSection> | ||
Revision as of 01:29, 9 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. |
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