Sandbox 43

From Proteopedia

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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.

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Trypsin

Trypsin is a serine protease that is used in the body to hydrolyze proteins. It is produced in the pancreas as its inactive zymogen form trypsinogen. It is produced inactively so as to not destroy the organ that produces it. Trypsin is used to cleave peptide bonds in proteins on the carboxyl side of the arginine or lysine. The exception to this is when either is followed by a proline, due to steric hindrance. Its optimal operating temperature is 37&deg C and around a pH of 8

Structure

Trypsin is composed of 229 amino acids. Its is composed of two alpha helices (pink) and two beta sheets (yellow). In addition to these patterns, trypsin has very distinct polar and nonpolar . The nonpolar areas are the hydrophobic molecules that are trying to stay away from water in the solvation sphere. The polar areas are hydrophilic and are on the outside of the molecule and interact with the solvation sphere.