Sandbox 14
From Proteopedia
Please do NOT make changes to this sandbox. Sandboxes 10-30 are currently reserved by Prof. Sheila Jaswal at Amherst College.
Trypsin
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Trypsin is a serine protease responsible for the breakdown of hydrolysis of proteins. This process is biologically applicable in the process of digestion. Trypsin like all other serine proteases is very specific in its reaction. It cleaves at peptide bonds after positive residues. These are arginine and lysine. The active site of trypsin is composed of a catalytic triad-Hs57,Asp102 and Cys 195. Each of these groups has a specific role to play in the hydrolysis of peptide bonds. The active site of trypsin can be found here. The S1 pocket of trypsin contains an aspartate residue which stabilizes the positive groups of the substrate. This process enhances the specificity of trysin.
Rat and bovine trypsin have been used for a variety of experimental procedures in the study of the serine protease trypsin. This paragraphs aims to identify any differences that might exist between rat and bovine trypsin paying attention to their active site. The structure of rat trypsin was shown above and can also be seen using this .Bovine trysin can be seen using this .
