6533b7d4fe1ef96bd12620e0
RESEARCH PRODUCT
Calorimetric study of myoglobin embedded in trehalose-water matrixes
Bellavia GAntonio CupaneLorenzo Cordonesubject
Ternary numeral systemChemistryHydrogen bondMineralogyCondensed Matter Physicschemistry.chemical_compoundDifferential scanning calorimetryChemical engineeringMyoglobinDenaturation (biochemistry)Physical and Theoretical ChemistryGlass transitionTernary operationThermal analysisdenaturation DSC glass transition myoglobin trehalosedescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2009-03-01 | Journal of Thermal Analysis and Calorimetry |