Sandbox 31
From Proteopedia
(Difference between revisions)
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==Structure== | ==Structure== | ||
<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)' /> | ||
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- | ===Secondary Structure=== | ||
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- | ===Polar vs Nonpolar Residues=== | ||
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- | ===Attractions of Structural Components=== | ||
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- | ===Ligands and Intermolecular Forces=== | ||
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+ | ==Secondary Structure== | ||
+ | ==Polar vs Nonpolar Residues== | ||
+ | ==Attractions of Structural Components== | ||
+ | ==Ligands and Intermolecular Forces== | ||
==Function== | ==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. | 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. |
Revision as of 18:41, 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
Structure
|
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.