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.