User:Bradley Duncan/Sandbox 1
From Proteopedia
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| - | <scene name='User:Bradley_Duncan/Sandbox_1/Scene_1/2'>Alpha-Chymotrypsin</scene> | ||
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| - | <scene name='User:Bradley_Duncan/Sandbox_1/Cationic_residues/1'>Cationic Residues</scene> | ||
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
| - | The dimer form of the protein (<scene name='User:Bradley_Duncan/Sandbox_1/Scene_1/2'>Alpha-Chymotrypsin</scene>) ). | ||
| - | + | Chymotrypsin (<scene name='User:Bradley_Duncan/Sandbox_1/Scene_1/2'>Alpha-Chymotrypsin Dimer</scene>) is a proteolytic enzyme which cleaves peptide bonds. The enzyme shows selectively to peptides with aromatic sidechains on the carboxyl side of the peptide bond. This is due to a “hydrophobic pocket” near the active site of the enzyme. The protein also contains a large number of cationic residues. | |
| + | In the this depiction <scene name='User:Bradley_Duncan/Sandbox_1/Cationic_residues/1'>Cationic Residues</scene>, these cationic amino acid residues on the protein (blue) can interact with anionic, functionalized nanoparticles. After the nanoparticle-protein complex is formed chymotrypsin then displays a preference for cationic substrates due to interaction with the anionic nanoparticle. The active site of chymotrypsin is shown in red. | ||
| - | A bacterial chemotaxis receptor is an unusually long alpha-helical structure. The attractant molecule (the ligand) binds near the top of this picture and sends a signal across the membrane into the cell to control proteins that bind near the bottom. This is a model of the structure of the receptor based on experimental structures of pieces of related proteins. | ||
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Revision as of 21:16, 30 April 2010
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
Chymotrypsin () is a proteolytic enzyme which cleaves peptide bonds. The enzyme shows selectively to peptides with aromatic sidechains on the carboxyl side of the peptide bond. This is due to a “hydrophobic pocket” near the active site of the enzyme. The protein also contains a large number of cationic residues.
In the this depiction , these cationic amino acid residues on the protein (blue) can interact with anionic, functionalized nanoparticles. After the nanoparticle-protein complex is formed chymotrypsin then displays a preference for cationic substrates due to interaction with the anionic nanoparticle. The active site of chymotrypsin is shown in red.
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Molecular Playground banner: Chymotrypsin is a digestive enzyme that breaks down proteins
