This project focuses on characterizing the stability of the High-Density Lipoprotein (HDL) molecule. HDL predominantly functions as a cholesterol transport molecule and has been shown to associate with a large number of additional proteins unrelated to this function. Here, we aim to understand how tightly these HDL-associated proteins interact with the HDL particle. This was done through the ICM Molsoft program where we performed protein-protein docking and found the binding energies for the HDL-associated proteins. ICM Molsoft uses a method called Optimal Docking area which predicts likely protein-protein interaction sites on protein surfaces, the software is then able to perform protein-protein docking to model how the HDL-associated proteins interact with the predominant structural protein on HDL (apoAI) to give us the binding energy. Our results showed a variety of binding energies and showed that some human proteins bind HDL either more tightly or more loosely than others. The proteins previously identified to reside on HDL that were tested included PON1, Compliment C3, apoA4, apoE, SAA1, apoC2, apoM, CETP, and Alpha 2 antiplasmin which showed binding energies ranging from -18.57 to -30.65 kcal/mol.