In 2020, 37.7 million individuals were living with HIV. If an individual infected with HIV does not undergo proper treatment, then the patient may obtain the disease acquired immunodeficiency syndrome. Although there are a myriad of HIV treatments and FDA-approved clinical inhibitors, drug resistance is the main obstacle to successful treatment plans. HIV protease is an essential protein that cleaves Gag and Gag-Pol polyproteins to yield infectious HIV. Due to HIV's rapid mutation, it is vital to develop more effective treatments and drugs for drug-resistant strains. X-ray crystallography and enzyme kinetics experiments are used to understand the binding of inhibitors to HIV proteases and aid the development of novel clinical inhibitors for resistant mutants of the protease. The binding of peptide analogs was studied for highly drug-resistant mutant PRS17 with a V48G mutation to wildtype residue. The revertant mutation showed small changes in inhibition or protease structure relative to PRS17.