Embedding biostructures in saccharide glasses protects them against extreme
dehydration and/or exposure to very high temperature. Among the saccharide
s, trehalose appears to be the most effective bioprotectant. In this paper
we report on the low-frequency dynamics of carbon monoxy myoglobin in an ex
tremely dry trehalose glass measured by neutron spectroscopy. Under these c
onditions, the mean square displacements and the density of state function
are those of a harmonic solid, up to room temperature, in contrast to D2O-h
ydrated myoglobin, in which a dynamical transition to a nonharmonic regime
has been observed at similar to 180 K (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 te
mperature.