A protein ligand has $10nM$ affinity for its binding partner. You mutate a serine residue on the ligand's

surface to an aspartic acid, which strengthens the electrostatic interaction with its binding partner by $1$

kca$\frac{l}{m}ol.$ What is the new affinity of the ligand for its binding partner? What assumptions did you make to

determine this affinity, and how will these assumptions impact the result?