A. You are performing experiments with your protein of interest and its ligand. You are attempting to mutate the binding site of
your protein to disrupt binding to ligand to see what happens inside the cell. You make a series of mutations and one in particular gives you surprising results: you observe that the mutation that you made in an amino acid that sticks out into the binding pocket actually increases the protein’s affinity for the ligand. Give a molecular explanation for these results
The ability of a protein to bind to its receptor depends on formation of noncovalent interactions with it. These interactions include hydrogen bonds, ionic bonds, van der Waals attractions and hydroph.
