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Sandbox 32
From Proteopedia
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=='''Introduction'''== | =='''Introduction'''== | ||
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<applet load='9PAP' size='600' frame='true' align='right' scene='Sandbox_32/Papain_default/7' caption='a' /> | <applet load='9PAP' size='600' frame='true' align='right' scene='Sandbox_32/Papain_default/7' caption='a' /> | ||
| - | + | '''Papain is a sulfhydrly protease from ''Carica papaya.''''' | |
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| + | Papain is a single chain protein of 212 residues and a molecular weight of 23.4kDa. About 7 <scene name='Sandbox_32/Alpha_helix/3'>alpha helices</scene> make up 25% of the secondary structure while 17 strands of <scene name='Sandbox_32/Beta_sheet/4'>beta sheets</scene> make up about 21%. Papain can be divided into <scene name='Sandbox_32/Domains_l_and_r/2'>two domains</scene>--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. | ||
| - | <scene name='Sandbox_32/ | + | The sulfhydryl protease contains many <scene name='Sandbox_32/hydrophobic residues/1'>hydrophobic residues</scene>. There are also a few <scene name='Sandbox_32/Negatively_charged_residues/1'> negatively charged</scene>residues and no positively charged residues except for histidine. Along with these hydrophobic/hydrophillic interactions, <scene name='Sandbox_32/disulfide_bonds/3'>disulfide bonds </scene> also are important structural components. There are 6 cysteine residues that form disulfide bonds at..... |
| - | <scene name='Sandbox_32/Catalytic_site/1'> | + | As a sulfhydrly protease, Papain has a catalytic site with three important residues--Cysteine-25, Histidine-159,and Asparganine176. The <scene name='Sandbox_32/Catalytic_site/1'>catalytic sited</scene> |
Revision as of 07:36, 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
