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Fast Dynamics and Stabilization of Proteins: Binary Glasses of Trehalose and Glycerol

Polymers Division, National Institute of Standards and Technology, Gaithersburg, Maryland

Correspondence: Address reprint requests to Marcus T. Cicerone, NIST, Polymers Division, 100 Bureau Dr., MS 8543, Gaithersburg, MD 20899-8543. Tel.: 301-975-8104; E-mail: cicerone{at}nist.gov.

We present elastic and inelastic incoherent neutron scattering data from a series of trehalose glasses diluted with glycerol. A strong correlation with recently published protein stability data in the same series of glasses illustrates that the dynamics at Q 0.71 Å^–1 and > 200 MHz are important to stabilization of horseradish peroxidase and yeast alcohol dehydrogenase in these glasses. To the best of our knowledge, this is the first direct evidence that enzyme stability in a room temperature glass depends upon suppressing these short-length scale, high-frequency dynamics within the glass. We briefly discuss the coupling of protein motions to the local dynamics of the glass. Also, we show that T_g alone is not a good indicator for the protein stability in this series of glasses; the glass that confers the maximum room-temperature stability does not have the highest T_g.

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