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Protein powders that are dehydrated or mixed with a glassy compound are known to have improved thermal stability. We present elastic and quasielastic neutron scattering measurements of the global dynamics of lysozyme and ribonuclease A powders. In the absence of solvation water, both protein powders exhibit largely harmonic motions on the timescale of the measurements. Upon partial hydration, quasielastic...
Glycerol has been shown to lower the heat denaturation temperature (Tm) of dehydrated lysozyme while elevating the Tm of hydrated lysozyme (Bell, Hageman, and Muraoka, 1995. J. Pharm. Sci. 84:707–712). Here, we report an in situ elastic neutron scattering study of the effect of glycerol and hydration on the internal dynamics of lysozyme powder. Anharmonic motions associated with structural relaxation...
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