Sandbox 38
From Proteopedia
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== '''History:''' == | == '''History:''' == | ||
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Papain was originally discovered during the colonial period in Congo. The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat. While they did not know the direct cause, this was when the proteolytic enzyme was first discovered. The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure. | Papain was originally discovered during the colonial period in Congo. The native inhabitants discovered that wrapping their elephant meat in papaya leaves helped to tenderize the meat. While they did not know the direct cause, this was when the proteolytic enzyme was first discovered. The active binding site of this enzyme was first discovered by Drenth et al., through the crystallographic analysis of the enzymes structure. | ||
== '''Composition of Papain:''' == | == '''Composition of Papain:''' == | ||
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Papain consists primarily of carbon, nitrogen, sulfur, and oxygen. The <scene name='Sandbox_38/Composition_of_papain/1'>composition of the enzyme</scene> can be view, as carbon is labled gray, oxygen red, nitrogen blue, and sulfur yellow. There are three <scene name='Sandbox_38/Disulfide_bridges/1'>disulfide bridges</scene> that contribute to the structure of Papain. These bonds are indicated by their yellow color, as they link particular cysteine residues. Throughout this enzyme, there are specific charged residues, indicating the most polar portions of the molecule. These <scene name='Sandbox_38/Charge/3'>charged residues</scene> can be visualized, as the cationic residues are blue in color, while the anionic residues are red. Partially charged residues are simply lighter in color. It is interesting to note that nearly all of these charged residues are located on the outer portion of the molecule in order to interact with the surrounding environment. | Papain consists primarily of carbon, nitrogen, sulfur, and oxygen. The <scene name='Sandbox_38/Composition_of_papain/1'>composition of the enzyme</scene> can be view, as carbon is labled gray, oxygen red, nitrogen blue, and sulfur yellow. There are three <scene name='Sandbox_38/Disulfide_bridges/1'>disulfide bridges</scene> that contribute to the structure of Papain. These bonds are indicated by their yellow color, as they link particular cysteine residues. Throughout this enzyme, there are specific charged residues, indicating the most polar portions of the molecule. These <scene name='Sandbox_38/Charge/3'>charged residues</scene> can be visualized, as the cationic residues are blue in color, while the anionic residues are red. Partially charged residues are simply lighter in color. It is interesting to note that nearly all of these charged residues are located on the outer portion of the molecule in order to interact with the surrounding environment. | ||
Revision as of 20:18, 13 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
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