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RESEARCH PRODUCT
Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature.
Eugenio VitranoGiuseppe ZaccaiLorenzo CordoneMichel Ferrandsubject
Drug CompoundingBiophysicsAnalytical chemistrychemistry.chemical_elementTrappingchemistry.chemical_compoundmedicineScattering RadiationDehydrationDeuterium OxideCryopreservationNeutronsMyoglobinSpectrum AnalysisTemperatureTrehaloseWatermedicine.diseaseTrehaloseNeutron spectroscopyCrystallographychemistryMyoglobinHarmonicDensity of statesGlassCarbonResearch Articledescription
Abstract Embedding biostructures in saccharide glasses protects them against extreme dehydration and/or exposure to very high temperature. Among the saccharides, trehalose appears to be the most effective bioprotectant. In this paper we report on the low-frequency dynamics of carbon monoxy myoglobin in an extremely dry trehalose glass measured by neutron spectroscopy. Under these conditions, the mean square displacements and the density of state function are those of a harmonic solid, up to room temperature, in contrast to D 2 O-hydrated myoglobin, in which a dynamical transition to a nonharmonic regime has been observed at ∼180K (Doster et al., 1989. Nature. 337:754–756). The protective effect of trehalose is correlated, therefore, with a trapping of the protein in a harmonic potential, even at relatively high temperature.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1999-02-01 | Biophysical journal |