This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox 44
From Proteopedia
(Difference between revisions)
| Line 20: | Line 20: | ||
<scene name='Sandbox_44/Hydrophobic_residues/1'>hydrophobic residues</scene> | <scene name='Sandbox_44/Hydrophobic_residues/1'>hydrophobic residues</scene> | ||
| + | |||
| + | <scene name='Sandbox_44/Chain_a/1'>chain A only</scene> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:09, 13 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. |
Lipase
PDB ID: 1HPLE.C.: 3.1.1.3
Number of Amino Acid Residues: 449
Number of Chains: 2
Introduction
The lipase class of enzymes are known to cut a lipid substrate at a specific location on their glycerol backbone. Pancreatic lipase, in particular, works to break down fats from the human diet. This lipase, therefore, is found in the digestive system of humans and is involved in the conversion of triglycerides to glycerides.
Structural Aspects of Lipase
| |||||||||||
