In the Shell Lab and Shea Lab, many research projects are being undertaken in collaboration to study protein interactions with molecular modeling. In particular, several of the projects study how water surrounding the protein binding sites impacts the binding process. In my project specifically, we characterized the hydrophobicity of the Receptor Binding Domain (RBD) for the SARS-CoV-2 spike protein to investigate the impact hydrophobicity plays in the binding between the spike protein and the ACE2 human receptor protein. Computational water triplet analysis proved to be a useful model to measure hydrophobicity of the Covid spike protein rather than directly analyzing the amino acids themselves. It led to some interesting early conclusions that hydrophobicity may be a more important factor in determining binding strength for certain variants of SARS-CoV-2 while perhaps being less of an influential factor in others.