Sandbox 31
From Proteopedia
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<applet scene='Sandbox_31/Trypsin_rainbow/1' size='225' frame='true' align='right' caption='The structure of trypsin in rainbow format. The N-terminus (blue) fades into the C-terminus (green)' /> | <applet scene='Sandbox_31/Trypsin_rainbow/1' size='225' frame='true' align='right' caption='The structure of trypsin in rainbow format. The N-terminus (blue) fades into the C-terminus (green)' /> | ||
| - | + | There are a few structural aspects that are very important to trypsin. In the image to the right, one can follow the lineage of the protein easily by tracing the protein from the N-terminus, which is colored blue, to the C-terminus, which is colored green. Other important aspects of this protein include: alpha helices, beta sheets, and the backbone. | |
Revision as of 20:12, 10 October 2010
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| 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. |
Contents |
Trypsin
Molecular Weight: 23.3 kDa
Structural Aspects
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There are a few structural aspects that are very important to trypsin. In the image to the right, one can follow the lineage of the protein easily by tracing the protein from the N-terminus, which is colored blue, to the C-terminus, which is colored green. Other important aspects of this protein include: alpha helices, beta sheets, and the backbone.
Secondary Structure
Polar vs Nonpolar Residues
Attractions of Structural Components
Ligands and Intermolecular Forces
Function
Trypsin hydrolyzes proteins and peptides. Trypsin acts on lysine and arginine; it cleaves the peptieds on the C-terminal side of the lysine and arginine residues.
