Calorimetric study of myoglobin embedded in trehalose-water matrixes

It has been suggested that in ‘dry’ protein-trehalose-water systems, water-mediated hydrogen bond network, whose strength increases by drying, anchors the protein to its surroundings. To further characterize this effect, we performed a DSC study on low-water myoglobin-trehalose systems. The denaturation temperature resulted to increase by decreasing hydration, and linearly correlated to the glass transition temperature of both the ternary protein-water-trehalose and the binary water-trehalose systems. Further measurements are being performed to investigate eventual differences among different saccharides.