Experimental Study of Dynamic Specific Heat Capacity of Protein Aqueous Solutions
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概要
- 論文の詳細を見る
We performed the measurements of the dynamic heat capacity of aqueoussolutions of lysozyme and a-chymotrypsin near heat denaturation by using an accalorimeter. The obtained values of the ac enthalpy and the ac entropy at theheat denaturation process were much smaller than those measured by usual dccalorimeters. This fact tells us that the main part of the dynamic denaturationprocess takes place at a frequency lower than our measuring frequency of 0.6 Hz,in consistent with the results given by T-jump experiments. Furthermore, it wasclarified by a circtular dichroism measurement that the disulfide bridges play animportant role in Itolding the three-dimensional structure of the proteins.
- 社団法人日本物理学会の論文
- 1981-01-15
著者
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MATSUDA Takashi
Department of Medicinal Chemistry, Kyoto Pharmaceutical University
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Hatta Ichiro
Department Of Applied Physics Faculty Of Engineering Nagoya University
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Imaizumi Shigeo
Department Of Applied Physics Faculty Of Engineering Nagoya University:suzuka College Of Technology
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Matsuda Takashi
Department Of Computer Science And Systems Engineering Kobe University
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Matsuda Takashi
Department Of Applied Physics Faculty Of Engineering Nagoya University
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Matsuda Takashi
Department Of Applied Mathematics And Physics Faculty Of Engineering Kyoto University
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Hatta Ichiro
Department of Applied Physics,Faculty of Engineering,Nagoya University
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