Sandbox 32
From Proteopedia
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Revision as of 23:17, 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
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Papain is a sulfhydrly protease from Carica papaya.
Papain is a single chain protein of 212 residues and a molecular weight of 23.4kDa. About 7 make up 25% of the secondary structure while 17 strands of make up about 21%. Papain can be divided into --an L and R domain (L=green and R=blue). Generally, the L domain contains many alpha-helical structural components while the R domain is characterized by anti-parallel beta sheet structure.
The sulfhydryl protease contains many . There are also a few residues and no positively charged residues except for histidine. Along with these hydrophobic/hydrophillic interactions, also are important structural components. There are 6 cysteine residues that form disulfide bonds at.....
As a sulfhydrly protease, Papain has a catalytic site with three important residues--Cysteine-25, Histidine-159,and Asparganine176. The
