Bulk aqueous solution has been the standard condition for studying protein stability. Inside the cell, however, large molecules are packed tightly, resulting in a highly crowded environment with limited space that may cause changes in protein thermodynamics. This crowded condition presents a wide range of spatial restriction, but it also presents opportunities for nonspecific interactions between proteins and their environment that may further alter stability. We are using reverse micelles to mimic the conditions presented by intracellular confinement. Reverse micelles are spontaneously organizing complexes with an aqueous core surrounded by a layer of surfactant dissolved in a nonpolar solvent. By encapsulating cytochrome c in the reverse micelle interior, we are using this system to examine the effects on protein stability. Cytochrome c denaturation is monitored by observing the intensity of the intrinsic tryptophan fluorescence which is quenched by the heme in the native state. By adjusting the pH of the system without affecting the composition of the reverse micelle shell, we can compare the influence of histidine protonation on stability as a function of the protein's environment. We examine this property using two surfactant mixtures of varying chemistry to extract the effects of nonspecific interactions with the interface on the thermodynamic stability of the protein. The results of our analysis will be presented and will show the differential effects of these important aspects of the protein's environment.