Sandbox 50: Difference between revisions
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=Trypsin= | =Trypsin= | ||
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== | |||
Trypsin's primary structure is a polypeptide chain of 237 amino acids. Trypsin has many important secondary structural units. The secondary structures can be seen in the adjacent figure | |||
