Sandbox 43: Difference between revisions
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<applet load='1QLQ' size='300' frame='true' align='right' caption='Insert caption here' /> | <applet load='1QLQ' size='300' frame='true' align='right' caption='Insert caption here' /> | ||
==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° C and around a pH of 8 | |||
==Structure== | |||
Trypsin is composed of 229 amino acids. Its <scene name='Sandbox_43/Trypsin_secondary_structure/1'>secondary structure</scene> is composed of two alpha helices (pink) and two beta sheets (yellow). | |||
Revision as of 03:24, 30 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.
TrypsinTrypsin 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° C and around a pH of 8 StructureTrypsin is composed of 229 amino acids. Its secondary structure is composed of two alpha helices (pink) and two beta sheets (yellow). |
