This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Sandbox 36
From Proteopedia
(Difference between revisions)
(Replacing page with '<!-- PLEASE DO NOT DELETE THIS TEMPLATE --> {{Template:Oberholser_Sandbox_Reservation}} <Structure load='9PAP' size='500' frame='true' align='right' caption='Introduction' scen...') |
|||
| Line 1: | Line 1: | ||
<!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | <!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | ||
{{Template:Oberholser_Sandbox_Reservation}} | {{Template:Oberholser_Sandbox_Reservation}} | ||
| - | <Structure load='9PAP' size='500' frame='true' align='right' caption=' | + | <Structure load='9PAP' size='500' frame='true' align='right' caption='Papain (9PAP)' scene='Insert optional scene name here' /> |
| + | ==Introduction== | ||
| + | '''Papain''' is a sulfhydryl protease derived from the papaya fruit. It consists of a single polypeptide chain of 212 amino acid residues folded into two domains. The active site is located in a groove between the two domains. The active site contains a catalytic diad made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis. | ||
| + | |||
<scene name='Sandbox_36/Helix_planes/1'>Hydrophobic Residues</scene> | <scene name='Sandbox_36/Helix_planes/1'>Hydrophobic Residues</scene> | ||
Revision as of 20:18, 11 November 2011
| 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. |
|
Introduction
Papain is a sulfhydryl protease derived from the papaya fruit. It consists of a single polypeptide chain of 212 amino acid residues folded into two domains. The active site is located in a groove between the two domains. The active site contains a catalytic diad made up of Cysteine-25 and Histidine-159. Aspartate-158 also plays a role in catalysis.
