3,4-Dihydroxyphenylalanine (Dopa) is a key component in mussel plaque adhesion. Dopa is a post-translational modification that heavily decorates many of the proteins found in adhesive plaques. However, when it is exposed to seawater, Dopa easily oxidizes to Dopa-quinone and loses its adhesive properties. Determining how mussels naturally protect Dopa can improve underwater adhesive technology because many commercially available adhesives and surgical adhesives mimicking mussel proteins fail due to oxidation. One of the ways mussels protect their Dopa-rich proteins is by secreting thiol-rich proteins along with them. The thiol groups act as reducing reservoirs for the Dopa-quinones, converting them back into Dopa. Furthermore, these proteins have been found to coacervate together and show a measurable increase in redox stability in coacervate phase. This study aims to determine the density, protein concentration, and water content of these coacervates such that the reducing capacity of the mussel plaque can be more efficiently mimicked. Density and water content will be determined by inducing coacervation with sulfate, spinning down the dense coacervate phase using centrifugation, and comparing the wet weight, freeze-dried weight, and volume of the samples. Protein concentration will then be determined using the Bradford assay.