Indicate the peptides that would result from cleavage by the indicated reagent: a. Gly-Lys-Leu-Ala-Cys-Arg-Ala-Phe by trypsin b. Glu-Ala-Phe-Gly-Ala-Tyr by chymotrypsin

a. Gly-Lys + Leu-Ala-Cys-Arg + Ala-Phe

b. Glu-Ala-Phe + Gly-Ala-Tyr

Explanation:

In this case, we have to remember which peptidic bonds can break each protease:

-) Trypsin

It breaks selectively the peptidic bond in the carbonyl group of lysine or arginine.

-) Chymotrypsin

It breaks selectively the peptidic bond in the carbonyl group of phenylalanine, tryptophan, or tyrosine.

With this in mind in "peptide a", the peptidic bonds that would be broken are the ones in the "Lis" and "Arg" (See figure 1).

In "peptide b", the peptidic bond that would be broken is the one in the "Phe" (See figure 2). The second amino acid that can be broken is tyrosine, but this amino acid is placed in the C terminal spot, therefore will not be involved in the hydrolysis.

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