I focus on predicting thermodynamic perturbations on membrane proteins (MPs). Many diseases are caused by mutations in MPs. I collaborate with the Schlebach lab at Indiana University to understand how mutations effect the structure, stability, and trafficking of G-protein coupled receptors. This work includes predicting stability changes of mutations in MPs. Predicting thermodynamic changes in MPs is a challenging task due to the complex environment of the membrane. Techniques used to experimentally measure stability changes depend on membrane mimetics, like detergent micelles, which can alter the stability of MPs. Structural data for MPs is often collected while the protein is in an environment geometrically and chemically different from its native environment; however, implicit membrane models fail to represent geometries of membrane mimetics. A portion of my work is to expand methods in Rosetta protein modeling suite to model MPs in membrane systems with different geometries.