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=='''References'''== | =='''References'''== | ||
| - | 1.Kamphuis, I. G., Kalk, K.H., Swarte, M.B., & Drenth, J (1984). Structure of papain refined at 1.65 A resolution. J. Mol. Biol. 179, 233-56. | + | 1. Kamphuis, I. G., Kalk, K.H., Swarte, M.B., & Drenth, J (1984). Structure of papain refined at 1.65 A resolution. J. Mol. Biol. 179, 233-56. |
| - | 2.Lowe, G. The structure and mechanism of action of papain (1970). Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257, 237-248. | + | 2. Lowe, G. The structure and mechanism of action of papain (1970). Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257, 237-248. |
| - | 3.PDB (2011). Retrieved November 10, 2011 from http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP | + | 3. PDB (2011). Retrieved November 10, 2011 from http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP |
| - | 4.PDBsum (2011). Retrieve November 12, 2011 from http://www.ebi.ac.uk/pdbsum/9pap | + | 4. PDBsum (2011). Retrieve November 12, 2011 from http://www.ebi.ac.uk/pdbsum/9pap |
| - | 5.Sathish, Hasige A., Kumar, Parigi Ramesh, & Prakash, Vishweshwaraiah (2009). The differential stability of the left and right domains of papain. Process Biochemistry. 44, 710-16. | + | 5. Sathish, Hasige A., Kumar, Parigi Ramesh, & Prakash, Vishweshwaraiah (2009). The differential stability of the left and right domains of papain. Process Biochemistry. 44, 710-16. |
Revision as of 01:24, 14 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
References
1. Kamphuis, I. G., Kalk, K.H., Swarte, M.B., & Drenth, J (1984). Structure of papain refined at 1.65 A resolution. J. Mol. Biol. 179, 233-56.
2. Lowe, G. The structure and mechanism of action of papain (1970). Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences. 257, 237-248.
3. PDB (2011). Retrieved November 10, 2011 from http://www.pdb.org/pdb/explore/explore.do?structureId=9PAP
4. PDBsum (2011). Retrieve November 12, 2011 from http://www.ebi.ac.uk/pdbsum/9pap
5. Sathish, Hasige A., Kumar, Parigi Ramesh, & Prakash, Vishweshwaraiah (2009). The differential stability of the left and right domains of papain. Process Biochemistry. 44, 710-16.
