Sandbox 35
From Proteopedia
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| - | == Introduction ==<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[9PAP]])' scene=''><scene name='Sandbox_35/Papain_trial_1/1'>TextToBeDisplayed</scene></StructureSection> | + | '''Papain''' is a sulfhydryl protease from the latex of the papaya fruit. Its molecules consist of one polypeptide chain with 212 amino acid residues. The chain is folded into two domains with the active site in a groove between the domains. |
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| + | == Introduction == | ||
| + | <StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[9PAP]])' scene=''><scene name='Sandbox_35/Papain_trial_1/1'>TextToBeDisplayed</scene></StructureSection> | ||
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| + | ==Your Heading Here (maybe something like 'Structure')==<StructureSection load='1dq8' size='500' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''>Anything in this section will appear adjacent to the 3D structure and will be scrollable.</StructureSection> | ||
Revision as of 01:50, 1 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. |
Papain is a sulfhydryl protease from the latex of the papaya fruit. Its molecules consist of one polypeptide chain with 212 amino acid residues. The chain is folded into two domains with the active site in a groove between the domains.
Introduction
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