User:Bradley Duncan/Sandbox 1
From Proteopedia
(df) |
m (k) |
||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | |||
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]. | ||
| Line 5: | Line 4: | ||
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. | 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 | + | |
| + | |||
| + | 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. | ||
| + | |||
| Line 15: | Line 17: | ||
Molecular Playground banner: Chymotrypsin is a digestive enzyme that breaks down proteins | 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. | ||
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.
|
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.
