A major challenge in the long-term management of HIV is drug resistance caused from high rate and error prone viral replication. To examine mechanisms of drug resistance within HIV-1 protease complexed with Darunavir, specific point mutations were placed in the protease amino acid sequence and molecular dynamic simulations were run. MATLAB and python scripts were developed to efficiently and consistently analyze simulation data. The team hypothesized that there would be a difference in inhibitor interactions and protein dynamic behavior in mutant variants compared to wild type. Although some aspects of increased resistance were seen with compounded mutations, overall this trend was not observed across every facet of our analysis
