Your PhD thesis project involves designing a drug that will bind specifically (v

Question

Your PhD thesis project involves designing a drug that will bind specifically (via complementary surfaces) to a mutant protein on tumor cells. This mutant protein has 6 consecutive stretches of 30 polar and charged amino acid side chains exposed to the outside of the tumor cell membrane.

5) Which of the following design features would you want to include in your drug to increase its affinity (attraction) for the mutant protein on the tumor cells?

a) methyl group

b) carboxyl group

c) hydroxyl groups

d) amino groups

e) any of the above except A

6) The mutant protein also possesses stretches of 30 hydrophobic amino acids located in between each of the stretches of polar and charged amino acid repeats, and their side chains are folded into the interior of folded protein. Which of the following plays the largest role in positioning those hydrophobic side chains in the interior of the protein?

a) ionic bonds between these side chains

b) quaternary structure bonds

c) van der Waals interactions between these side chains

d) disulfide bonds

e) lack of hydrogen bonding of these side chains with water

Explanation / Answer

5. Option E is correct.
Like dissolves like: A hydrophobic group interacts with a hydrophobic group. A hydrophilic group interacts with a hydrophilic group.
Since the protein surface contains hydrophilic groups, the drug should contain hydrophilic groups such as carboxyl, hydroxyl, and amino groups.

6. Option C is correct.
Hydrophobic groups are stacked together by Vander Wal interactions.

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