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Sandbox 44
From Proteopedia
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<applet load='1QLQ' size='300' frame='true' align='right' caption='Bovine Pancreatic Trypsin' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Bovine Pancreatic Trypsin' /> | ||
| + | =Trypsin= | ||
| + | Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine is located in the active site of the molecule. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen. | ||
| + | ==Structural Aspects== | ||
| + | |||
| + | ==Function== | ||
Here is shown the hydrophobic vs hydrophilic <scene name='Sandbox_44/Hydrophilic_vs_polar_residues/2'>structure</scene> of the protein. Polar molecules appear yellow, while nonpolar appear light purple. | Here is shown the hydrophobic vs hydrophilic <scene name='Sandbox_44/Hydrophilic_vs_polar_residues/2'>structure</scene> of the protein. Polar molecules appear yellow, while nonpolar appear light purple. | ||
This is the <scene name='Sandbox_44/Secondary_structure_of_trypsin/1'>Secondary</scene> Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.) | This is the <scene name='Sandbox_44/Secondary_structure_of_trypsin/1'>Secondary</scene> Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.) | ||
Revision as of 23:09, 27 October 2010
| 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
Trypsin is a serine protease that is produced in the pancreas. Serine protease means that it is an enzyme that cleaves amino acid sequences and that a serine is located in the active site of the molecule. In order to prevent it from breaking down the proteins in the pancreas of the organism that produces it, it is first produced as the inactive zymogen, proenzyme trypsinogen.
Structural Aspects
Function
Here is shown the hydrophobic vs hydrophilic of the protein. Polar molecules appear yellow, while nonpolar appear light purple.
This is the Structure of trypsin is displayed.(The pink-alpha helix, and the yellow-beta sheets.)
