Intrinsically disordered proteins (IDPs) are proteins that do not fold into a fixed structure. Such proteins participate in a phenomenon known as phase separation, where they can self-associate to form regions with distinct properties. This compartmentalization of biomolecules is a key feature in many biological processes, and their emergent properties in the presence of small molecules. In particular, we utilize molecular dynamics (MD) simulations to examine how different buffer molecules interact with IDPs. Using atomistic MD simulations, we can examine interactions between individual solvent and co-solvent molecules and specific amino acid residues. These interactions are present for buffers in research lab settings as well as excipients in drug development and formulation. By examining these interactions, we aim to get a better understanding of how the properties of IDPs and the surrounding area are affected by these additional molecules.
