Dielectric relaxation of a proton glass in hydrated protein powders

Dielectric relaxation in the kHz to MHz range displayed by hydrated powders of the protein lysozyme at room temperature is mainly due to protons migrating between ionized side chains. Quite recently we have measured the frequency and temperature dependence of this relaxation, and we have detected th...

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Bibliographic Details
Published inSolid state ionics Vol. 125; no. 1-4; pp. 257 - 261
Main Authors Careri, G, Consolini, G, Bruni, F
Format Journal Article Conference Proceeding
LanguageEnglish
Published Amsterdam Elsevier B.V 01.10.1999
Elsevier Science
Subjects
Biological and medical sciences
Dielectric
Fundamental and applied biological sciences. Psychology
Glass
Hydration
Miscellaneous
Molecular biophysics
Physico-chemical properties of biomolecules
Protein
Proton
Proton
Hydration
Dielectric
Protein
Glass
Enzyme
Glycosidases
Hydrolases
O-Glycosidases
Lysozyme
Dielectric relaxation
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Summary:Dielectric relaxation in the kHz to MHz range displayed by hydrated powders of the protein lysozyme at room temperature is mainly due to protons migrating between ionized side chains. Quite recently we have measured the frequency and temperature dependence of this relaxation, and we have detected the freezing to a broad distribution of relaxation times, typical of proton glasses. Below the freezing temperature of about 270 K the system is not ergodic, in analogy with the behavior of proton glass crystals made up by random mixtures of ferro- and antiferroelectric compounds.
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ISSN:0167-2738
1872-7689
DOI:10.1016/S0167-2738(99)00183-6