Abstract:
: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 >or= 0.71 A(-1) and omega > 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).
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Cicerone MT,Soles CLdoi
10.1529/biophysj.103.035519subject
Has Abstractpub_date
2004-06-01 00:00:00pages
3836-45issue
6eissn
0006-3495issn
1542-0086pii
S0006-3495(04)74424-0journal_volume
86pub_type
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