How the primary sequence of amino acids determines a protein's folding free energy landscape remains elusive. Pressure denaturation permits a unique approach to study protein folding as its primary effects are local, due to the elimination of cavities present in the folded structure upon unfolding. This local nature of pressure denaturation leads to increased probability of populating folding intermediates compared to chemical or heat denaturation. We examined a leucine rich repeat protein, PP32, which presents high folding cooperativity in urea melts and displays increasing stability from the N- to C-terminus. Cavity forming Leucine/Isoleucine to Alanine mutations of PP32 were made to test the effects of cavities on the folding free energy landscape. The mutant protein folding properties were observed via pressure-jump (p-jump) fluorescence and high pressure (HP) NMR. P-jump fluorescence experiments yielded the equilibrium volume change and activation volumes for folding and unfolding. The latter were consistent with an unfolding mechanism by which the main cavity of PP32 is disrupted at the barrier, and the remaining smaller cavities are eliminated after the rate limiting step. HP 2D NMR measurements at equilibrium, coupled to constrained coarse grained simulations, yielded pseudo free energy profiles and structural information of the PP32 ensemble at different pressures. Our results demonstrate how mutations modulate the asymmetric stability of this protein, and the consequences of this modulation on the cooperativity of the transition.