User:Bradley Duncan/Sandbox 1
From Proteopedia
(d) |
(d) |
||
| Line 8: | Line 8: | ||
In this depiction of the monomer <scene name='User:Bradley_Duncan/Sandbox_1/Cationic_residues/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. | In this depiction of the monomer <scene name='User:Bradley_Duncan/Sandbox_1/Cationic_residues/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. | ||
| + | |||
| + | ===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. | ||
{{Clear}} | {{Clear}} | ||
Revision as of 21:23, 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 this depiction of the monomer , 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.
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.
|
Molecular Playground banner: Chymotrypsin is a digestive enzyme that breaks down proteins
