Molecular playground/Chymotrypsin
From Proteopedia
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{{STRUCTURE_4cha | PDB=4cha| SCENE=User:Bradley_Duncan/Sandbox_1/Scene_1/2 }} | {{STRUCTURE_4cha | PDB=4cha| SCENE=User:Bradley_Duncan/Sandbox_1/Scene_1/2 }} | ||
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| - | In this depiction | + | 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. |
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Current revision
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| 4cha, resolution 1.68Å () | |||||||||
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| Activity: | Chymotrypsin, with EC number 3.4.21.1 | ||||||||
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| Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
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.
