User:Bradley Duncan/Sandbox 1
From Proteopedia
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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]. | |
| - | <scene name='User:Bradley_Duncan/Sandbox_1/Cationic_residues/1'>Cationic Residues</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. | |
| - | 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>) ). | ||
| - | + | In this depiction, <scene name='User:Bradley_Duncan/Sandbox_1/Cbi/1'>Cationic Residues</scene>, the 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. | ||
{{Clear}} | {{Clear}} | ||
<applet load='1wat' size='[450,338]' frame='true' align='right' | <applet load='1wat' size='[450,338]' frame='true' align='right' | ||
| - | caption=' | + | caption='Structure of Alpha-Chymotrypsin (4cha)' scene='User:Bradley_Duncan/Sandbox_1/Scene_1/2'/> |
| - | === Ligand-binding domain === | ||
| + | Molecular Playground banner: Chymotrypsin is a digestive enzyme that breaks down proteins | ||
| + | ===References=== | ||
| - | + | You C-C, Agasti SS, De M, Knapp MJ, Rotello VM. Modulation of the Catalytic Behavior of α-Chymotrypsin at Monolayer-Protected Nanoparticle Surfaces. Journal of the American Chemical Society 2006; 128:14612-14618. | |
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Current revision
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 this depiction, , the 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
References
You C-C, Agasti SS, De M, Knapp MJ, Rotello VM. Modulation of the Catalytic Behavior of α-Chymotrypsin at Monolayer-Protected Nanoparticle Surfaces. Journal of the American Chemical Society 2006; 128:14612-14618.
