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231222s1999 xx ||||| 00| ||eng c |
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|a pubmed25n0395.xml
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|a (DE-627)NLM118498576
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|a (NLM)11970721
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|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Levstik, A
|e verfasserin
|4 aut
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|a Proton glass freezing in hydrated lysozyme powders
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|c 1999
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|b nc
|2 rdacarrier
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|a Date Completed 09.08.2002
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|a Date Revised 28.07.2019
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|a published: Print
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Powders
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|a Protons
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|a Water
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|a 059QF0KO0R
|2 NLM
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|a Muramidase
|2 NLM
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|a EC 3.2.1.17
|2 NLM
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| 700 |
1 |
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|a Filipic, C
|e verfasserin
|4 aut
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| 700 |
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|a Kutnjak, Z
|e verfasserin
|4 aut
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| 700 |
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|a Careri, G
|e verfasserin
|4 aut
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|a Consolini, G
|e verfasserin
|4 aut
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|a Bruni, F
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics
|d 1993
|g 60(1999), 6 Pt B vom: 30. Dez., Seite 7604-7
|w (DE-627)NLM098226002
|x 1063-651X
|7 nnns
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| 773 |
1 |
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|g volume:60
|g year:1999
|g number:6 Pt B
|g day:30
|g month:12
|g pages:7604-7
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|d 60
|j 1999
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