Proton glass freezing in hydrated lysozyme powders
At room temperature, the dielectric relaxation of hydrated powder of the protein lysozyme is known to be due to protons migrating between ionized side chains. A recent study of this relaxation at lower temperatures suggested a behavior typical of proton glasses. An analysis of the complex dielectric...
| Veröffentlicht in: | Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics. - 1993. - 60(1999), 6 Pt B vom: 30. Dez., Seite 7604-7 |
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| 1. Verfasser: | |
| Weitere Verfasser: | , , , , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
1999
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| Zugriff auf das übergeordnete Werk: | Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics |
| Schlagworte: | Journal Article Powders Protons Water 059QF0KO0R Muramidase EC 3.2.1.17 |
| Zusammenfassung: | At room temperature, the dielectric relaxation of hydrated powder of the protein lysozyme is known to be due to protons migrating between ionized side chains. A recent study of this relaxation at lower temperatures suggested a behavior typical of proton glasses. An analysis of the complex dielectric susceptibility by a temperature-frequency plot presented here has revealed that ergodicity is broken due to the divergence of the longest relaxation time at 266 K, indicating specifically that this hydrated protein is a proton glass. A change in the temperature behavior of the static dielectric constant and the average relaxation frequency at 273 K indicates a further transition occurring at this temperature, whose nature remains to be investigated |
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| Beschreibung: | Date Completed 09.08.2002 Date Revised 28.07.2019 published: Print Citation Status MEDLINE |
| ISSN: | 1063-651X |