Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at...

Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at the C-terminal end of specific residues. Chymotrypsin recognizes aromatic residues, while trypsin recognizes lysine and arginine. The recognition of a particular side chain (side chain specificity) is fully determined by the structure and properties of the binding pocket. In the case of chymotyipsin the binding pocket is hydrophobic and is wide enough to accommodate an aromatic ring. Given what you know about the properties of Lys/Arg side chains, what can you say about the size/shape and possible interactions that would provide the substrate specificity in the case of trypsin? What amino acid residues from the trypsin molecule would you expect to find in the binding site?

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queen_honey_blossom answered 1 year ago

Trypsin is a proteolytic enzyme that displays a similar mechanism to the studied for chymotrypsin (serine...

Trypsin is a proteolytic enzyme that displays a similar mechanism to the studied for chymotrypsin (serine protease). Tosyl-L-lysine chloromethyl ketone is a specific inhibitor of trypsin. Why is this compound specific for trypsin?

How do serine proteases hydrolyze dietary proteins? Describe the catalytic activity of chymotrypsin.

Which is true about Trypsin? It does not affect any peptide bonds. It hydrolyzes all peptide...

Which is true about Trypsin? It does not affect any peptide bonds. It hydrolyzes all peptide bonds. It hydrolyzes peptide bonds to leucine and phenylalanine. It hydrolyzes peptide bonds to arginine and lysine.

4. The S1 pocket of serine proteases a. is where the proper substrate binds b. is...

4. The S1 pocket of serine proteases a. is where the proper substrate binds b. is the catalytic triad c. determines which amino acid side chain is bound d. all of the are true e. none of the above are true 5. With respect to aspartyl proteases a. the use a zinc to make alkoxide b. they use an activated hydroxyl made from water c. they form a transient covalent bond with the peptide being cut d. all the above...

A sample of a peptide of unknown sequence was treated with trypsin; another sample of the...

A sample of a peptide of unknown sequence was treated with trypsin; another sample of the same peptide was treated with chymotrypsin. The sequences (N-terminal to C-terminal) of the smaller peptides produced by trypsin digestion were as follows: Cys—Thr—Ala—Ser—Ile—Lys Arg—Thr—Arg—Gln—Arg Gln—Phe—Ala—Val—Tyr—Asn—Lys Phe—His—Cys—Asn The sequences of the smaller peptides produced by chymotrypsin digestion were as follows: Asn—Lys—Cys—Thr—Ala—Ser—Ile—Lys—Phe Arg—Thr—Arg—Gln—Arg—Gln—Phe His—Cys—Asn Ala—Val—Ty

Endo/lysosomal proteases cleave proteins at different positions than the proteasome. Peptides generated by the vacuolar pathway...

Endo/lysosomal proteases cleave proteins at different positions than the proteasome. Peptides generated by the vacuolar pathway can be expected to differ from those generated by the cytosolic pathway. Why might this be a problem for cytolytic T cell responses?

Why are the peptide fragments generated by trypsin digestion incompatible with C-terminal sequencing using carboxypeptidase A?

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Trypsin and chymotrypsin are members of the family of serine proteases. They cleave peptide bonds at...

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