Recent advances in computational protein design and structure prediction have empowered a new age of protein science and engineering. These techniques can help to visualize structures that were previously unsolvable, provide insights into protein-protein interactions, and yield the design of entirely new agents. One key challenge in implementation of these approaches is the technical accessibility for groups with minimal computational experience as they work to become successful users of the variety of tools available. In this talk, I will discuss my group’s efforts to design and implement minimalist in silico protein engineering approaches to generate protein libraries with the goal of accessibility to users with varied computational experience. These libraries are implemented experimentally and compared to random amino acid variation to determine if minimalist in silico library design is a superior approach. Characterization of affinity, stability, and function of variants generated from both approaches will be discussed.