The non-invasive and non-destructive determination of numerous physicochemical properties of protein therapeutics and their aggregates is critical for developing formulation conditions that enhance product efficacy, stability and manufacturability. Moreover, to meet the analytical challenges in early stage development, where the amount of material is limited, tools that measure very small volumes are also highly desirable. In this presentation I will describe a new analytical tool that can work with small amounts of protein samples to rapidly and simultaneously measure relative protein molecular structure and size (including aggregation) over a range of concentrations and formulation conditions. The technique uniquely combines two well-established analytical techniques namely dynamic light scattering (DLS) and Raman spectroscopy to derive structural, thermodynamic and kinetic insights into the mechanisms of protein aggregation and the factors that influence protein stability. I will present a number of examples using model systems and manufactured biopharmaceutical products to illustrate the synergies of the two techniques and the new insights afforded by the combined approach.