Sandbox 31

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Papain is formed from a peptide that is 212 amino acids in length. It consists of 25% <scene name='Sandbox_31/Alpha_helices/3'>Alpha helices</scene> and 21% <scene name='Sandbox_31/Beta_sheet/1'> Beta sheet</scene>. The structure also consists of three <scene name='Sandbox_31/Disulfide/2'>disulfide bonds</scene> between cysteine residues. Another important residue to the structure is Cysteine 25 which has a sulfhydryl group that plays a major role in the active site activity[[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html]].
Papain is formed from a peptide that is 212 amino acids in length. It consists of 25% <scene name='Sandbox_31/Alpha_helices/3'>Alpha helices</scene> and 21% <scene name='Sandbox_31/Beta_sheet/1'> Beta sheet</scene>. The structure also consists of three <scene name='Sandbox_31/Disulfide/2'>disulfide bonds</scene> between cysteine residues. Another important residue to the structure is Cysteine 25 which has a sulfhydryl group that plays a major role in the active site activity[[http://www.sigmaaldrich.com/life-science/metabolomics/enzyme-explorer/analytical-enzymes/papain.html]].
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The <scene name='Sandbox_31/Hydrophobic_residues/1'>Hydrophobic Residues</scene> in papain are primarily located toward the inside of the enzyme or paired by hydrophobic interactions with other hydrophobic residues to exclude water. The <scene name='Sandbox_31/Charged/1'>Charged Residues</scene> are located facing the exterior, in the active site, or paired with other charged residues.
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<scene name='Sandbox_31/Hydrophobic_residues/1'>Hydrophobic Residues</scene>
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</StructureSection>
</StructureSection>

Revision as of 20:27, 6 November 2011

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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 (PDB ID #: 9pap)

Structure of HMG-CoA reductase (PDB entry 9pap)

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