Fast dynamics and stabilization of proteins: binary glasses of trehalose and glycerol.

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 J

journal_title

Biophysical journal

authors

Cicerone MT,Soles CL

doi

10.1529/biophysj.103.035519

subject

Has Abstract

pub_date

2004-06-01 00:00:00

pages

3836-45

issue

6

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(04)74424-0

journal_volume

86

pub_type

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