This study looks at the influence of reduced levels of hydration as a driving force for transitions in the secondary structure of hydrated proteins. A simple protein-water system was used to study the conditions of typical protein-rich dairy food systems at a fixed pH level, salt content, and temperature. Freezedried beta-lactoglobulin (Type A) from bovine milk was dissolved directly into two different buffer systems over a wide range of concentrations between 1 mg/ml (~54 mM) and 200 mg/ml (~0.01 M) but at a fixed pH level, pH 3. Circular dichroism (CD), attenuated total reflectance Fourier transform infrared spectroscopy (ATR FTIR), and thioflavin T (ThT) Assay fluorescence spectroscopy were used to measure changes in the secondary structure with respect to protein solution concentration at 20 C. The findings of all of the techniques indicate that the majority of the secondary structure changes occur within the low protein concentration regime (i.e. <50 mg/ml) before a critical aggregation threshold. Dimerisation, formed by besheet cross-linking, is the likeliest mechanism of aggregation. The formation of dimers however counters the current assumption that at pH 3 only monomers exist; rather it seems there is a gradual evolution of the monomeric unfolded state with increasing concentration occurs yielding a bsheet rich refolded aggregate. Most interesting is the low concentration region (i.e. between 1 mg/ml and 40 mg/ml) where most secondary structural alterations are found to occur; before physical crowding effects are possible. The results indicate that BLG has a limited solubility even in a low concentration regime.