The signicant α-helical content of HSA will have an eect, as the conguration in space will aect both the accessibility of specic residues, and the local environment in which they reside. This is represented in MARTINI as a change in the polarity of the backbone bead of all residues present in a helix as well as the side chains of glycine, alanine and protein, α-helix will have signicantly less hydrophobic character than one outside of a helix. As 87.5% of the APRs are found within α-helices and 39.1% of the residues within the helices are APRs, it is likely that the interaction between helices and excipient, or helices and solvent is signicant in aggregation prevention. Indeed, α-helices have been shown to induce the formation of protein aggregates.