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A statistical mechanical theory is presented to predict the effects ofmacromolecular crowding on protein association equilibria, accounting for bothexcluded volume and attractive interactions between proteins and crowdingmolecules. Predicted binding free energies are in excellent agreement withsimulation data over a wide range of crowder sizes and packing fraction. It isshown that attractive interactions between proteins and crowding agentscounteract the stabilizing effects of excluded volume interactions. A criticalattraction strength, for which there is no net effect of crowding, is almostindependent of the crowder packing fraction.

Crowding induced entropy-enthalpy compensation in protein association equilibria