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.
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. |
