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Trypsin is a medium sized, globular, digestive serine protease that is synthesized by the pancreas and secreted into the duodenum of the small intestine. Trypsin hydrolyzes peptide bonds based on side chain specificities of the amino acids surrounding the bond to be cleaved. Trypsin's specificity is for the positively charged side chains of lysine and arginine. | Trypsin is a medium sized, globular, digestive serine protease that is synthesized by the pancreas and secreted into the duodenum of the small intestine. Trypsin hydrolyzes peptide bonds based on side chain specificities of the amino acids surrounding the bond to be cleaved. Trypsin's specificity is for the positively charged side chains of lysine and arginine. | ||
==Structure== | ==Structure== | ||
Trypsin's primary structure is a polypeptide chain of 237 amino acids. Trypsin has many important secondary structural | Trypsin's primary structure is a polypeptide chain of 237 amino acids. Trypsin has many important <scene name='Sandbox_50/Secondarystructure/1'>secondary structural elements</scene>, including two alpha helices (blue) and an anti-parallel beta sheet. | ||
Revision as of 05:36, 29 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
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