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Sandbox 36
From Proteopedia
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| - | <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. | ||
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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. |
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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.
