Proteins tend to misfold and adhere to artificial surfaces, limiting our ability to employ proteins and their many functions in technologies. Understanding the physics behind such surface-induced protein misfolding would enable design of improved biocompatible surfaces on which proteins retain their structure and function. Such materials could be used to design new protein-based biosensors for detection of a variety of biomarkers. Thus motivated, I aim to experimentally determine the origins of surface-induced protein adsorption and misfolding using a new, quantitative, technique to measure the thermodynamic stability of surface-tethered proteins. To this end, I have designed, produced, and purified proteins that can be site-specifically attached to surfaces, and characterized their thermodynamic stability in bulk solution. Comparison of the stability of the protein in solution to that of the surface-tethered protein will inform on the effect surfaces have on protein structure and function. Ultimately, I expect my work to lead to the first high-precision measurements of how artificial surfaces affect protein function and stability. These results can then be used to build new, quantitative theoretical models of protein-surface interactions, models that ultimately can be used to guide rational design of new artificial surfaces that are optimally compatible with protein structure and function.