BCH210H1 Lecture Notes - Lecture 3: Trypsin, Carboxypeptidase, Tryptophan
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You wish to design a new serine protease that will cleave polypeptide chains to create a series of fragments that contain either cysteine or serine residues at their C-termini. Which of the following characteristics of the new protease is most important to achieve this result?
A. | The protease should have an oxyanion hole that is capable of binding only to cysteine side chains. | |
B. | The protease should have a specificity pocket that can accommodate only small, uncharged polar side chains. | |
C. | The protease should have a specificity pocket that can accommodate only small negatively charged side chains. | |
D. | The protease should be able to form hydrogen bonds to the side chains of the cysteine residues in the substrate polypeptide that do not form with other amino acids. | |
E. | The protease should be able to form irreversible disulfide bonds to the cysteine residues in the substrate polypeptide. |