chymotrypsin useful shit - Chymotrypsin serine protease...

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Chymotrypsin – serine protease that cleaves a peptide that has an aromatic amino acid. So that’s what it needs to do It stabilizes the transition state. The least stable transition state that you have in chymotryypsin is the tetrahedral intermediate. Function 1) catalysis – serine attacks and forms the tetrahedral intermediate 2) stabilize – stabilize this very unstable tetrahedral intermediate. 3) Bind to peptides that have a very large hydrophobic residue Have inactive form of chymotrypsin – which is chymotrypsinogen, secreted in pancreas. Only becomes activated when in the stomach Things to pay attention to 1) how does cleave from chymotrypsinogen to chymo make the enzyme active 2) how does chymotrypsin catalyze the cleavage of the peptide bond. What are aa necessary for cleavages 3) how does chymotrypsin stabilize the unstable transition state of the tetrahedral intermediate 4) how does chymotrypsin bind to specifically with large hydrophobic amino
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chymotrypsin useful shit - Chymotrypsin serine protease...

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