You are planning a chromatographic separation using a "fast" affinity adsorbent, meaning it has a binding kinetics allowing elution chromatography based on rapid local equilibrium. You have prepared the chromatography based on separate measurements of the interaction between the affinity ligand L and proteins A and B from one extract, as well as proteins X and Y from another extract. Chromatography and measurements are conducted at $25\backslash$deg C$.$ The ligand concentration $($m$)$ on the affinity gel is $1\mathrm{.}0*10^-5$ M$.$

Table:

Protein : Molar Free Energy $(\backslash$Delta G$)$ for Dissociation of Protein$-$Ligand Complex

A: $23\mathrm{.}0$ kJ

B: $17\mathrm{.}0$ kJ

X: $28\mathrm{.}7$ kJ

Y: $31\mathrm{.}2$ kJ

The column's resolution capacity is approximately $100$ theoretical plates. Discuss and explain, based on the given data, whether the pair A$/$B or the pair X$/$Y has the best chances of being well$-$separated under the given condition