Dielectric relaxation of a proton glass in hydrated protein powders

被引:11
作者
Careri, G
Consolini, G
Bruni, F
机构
[1] Univ Roma La Sapienza, Dipartimento Fis, INFM, Unita Roma Uno, I-00185 Rome, Italy
[2] CNR, Ist Fis Spazio Interplanetario, I-00133 Rome, Italy
[3] Univ Roma Tre, INFM, Dipartimento Fis E Amaldi, Unita Roma Tre, I-00146 Rome, Italy
关键词
dielectric; glass; protein; proton; hydration;
D O I
10.1016/S0167-2738(99)00183-6
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
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. (C) 1999 Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码:257 / 261
页数:5
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