Measurements of thermal conductivity and thermal diffusivity of hen egg-white lysozyme crystals using a short hot wire method

Thermal conductivity and thermal diffusivity of hen egg-white lysozyme (HEWL) crystals were examined by using the transient short hot wire method. This method is based on the conventional hot wire method, but improved by using a wire that is much shorter than conventional ones. The magneto-Archimede...

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Bibliographic Details
Published inAIP conference proceedings Vol. 1865; no. 1
Main Authors Fujiwara, Seiji, Maki, Syou, Tanaka, Seiichi, Maekawa, Ryunosuke, Masuda, Tomoki, Hagiwara, Masayuki
Format Journal Article Conference Proceeding
LanguageEnglish
Published Melville American Institute of Physics 21.07.2017
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Summary:Thermal conductivity and thermal diffusivity of hen egg-white lysozyme (HEWL) crystals were examined by using the transient short hot wire method. This method is based on the conventional hot wire method, but improved by using a wire that is much shorter than conventional ones. The magneto-Archimedes levitation technique was utilized to attach the HEWL crystals onto the wire. Owing to the upward magnetic force, the HEWL crystals were deposited at the air-liquid interface of the protein buffer solution where the short hot wire was preliminarily fixed. In situ observation clarified that the wire was completely buried into the HEWL crystals. By means of these techniques, the measurement of thermal conductivity and thermal diffusivity of HEWL crystals was realized for the first time. Gadolinium chloride (a paramagnetic subject) was used as a precipitant agent of crystallization. Crystal growth was carried out over 20 h at 17.2 °C. The applied magnetic field was 4 T. Measurements were conducted during the crystal growth at two different times. The thermal conductivity and diffusivity of the HEWL crystals were determined to be 0.410 W/(m·K) and 3.77×10−8 m2/s at 14 h after, and 0.438 W/(m·K) and 5.18×10−8 m2/s at 20 h after, respectively. We emphasize that this method is versatile and applicable for other protein crystals.
Bibliography:ObjectType-Conference Proceeding-1
SourceType-Conference Papers & Proceedings-1
content type line 21
ISSN:0094-243X
1551-7616
DOI:10.1063/1.4993351