Proton freezing in hydrated lysozyme powders

The dielectric relaxation of hydrated powder of the protein lysozyme has suggested a behavior typical of proton glasses. An analysis by a temperature-frequency plot presented here revealed that ergodicity would be broken due to the divergence of the longest relaxation time at 266 K, thus indicating...

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Bibliographic Details
Published inFerroelectrics Vol. 240; no. 1; pp. 1555 - 1561
Main Authors Levstik, A., Filipič, C., Kutnjak, Z., Careri, G., Consolini, G., Bruni, F.
Format Journal Article
LanguageEnglish
Published Taylor & Francis Group 01.01.2000
Subjects
Dielectric
glass
hydration
proteins
relaxation
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Summary:The dielectric relaxation of hydrated powder of the protein lysozyme has suggested a behavior typical of proton glasses. An analysis by a temperature-frequency plot presented here revealed that ergodicity would be broken due to the divergence of the longest relaxation time at 266 K, thus indicating that this hydrated protein belongs indeed to a proton glass family. However, the temperature behavior of the static dielectric constant and the average relaxation frequency indicates a transition near 273 K which precedes the glassy freezing transition. This transition deserves further study, since it seems that its origin cannot be trivially connected to the formation of bulk ice.
ISSN:0015-0193
1563-5112
DOI:10.1080/00150190008227982