3 0 0 0 OA 深夜アニメのトラウマ構造 ―最終戦争の破局は回避されるのか
- 著者
- 森 年恵 森 茂起 木下 雅博 Toshie MORI Shigeyuki MORI Masahiro Kinoshita
- 出版者
- 甲南大学人間科学研究所
- 雑誌
- 心の危機と臨床の知
- 巻号頁・発行日
- vol.21, pp.19-29, 2020-03-20
- 著者
- Masahiro Kinoshita
- 出版者
- The Biophysical Society of Japan
- 雑誌
- Biophysics and Physicobiology (ISSN:21894779)
- 巻号頁・発行日
- vol.18, pp.60-66, 2021 (Released:2021-03-27)
- 参考文献数
- 17
- 被引用文献数
- 2 2
- 著者
- Koji Oda Masahiro Kinoshita
- 出版者
- 一般社団法人 日本生物物理学会
- 雑誌
- Biophysics and Physicobiology (ISSN:21894779)
- 巻号頁・発行日
- vol.12, pp.1-12, 2015 (Released:2015-07-31)
- 参考文献数
- 47
- 被引用文献数
- 4 11
There is an empirical rule that the thermal stability of a protein is related to the packing efficiency or core volume of the folded state and the protein tends to exhibit higher stability as the backbone and side chains are more closely packed. Previously, the wild type and its nine mutants of staphylococcal nuclease were compared by examining their folded structures. The results obtained were as follows: The stability was not correlated with the number of intramolecular hydrogen bonds, intramolecular electrostatic interaction energy, or degree of burial of the hydrophobic surface; though the empirical rule mentioned above held, it was not the proximate cause of higher stability; and the number of van der Waals contacts NvdW, or equivalently, the intramolecular van der Waals interaction energy was an important factor governing the stability. Here we revisit the wild type and its nine mutants of staphylococcal nuclease using our statistical-mechanical theory for hydration of a protein. A molecular model is employed for water. We show that the pivotal factor is the magnitude of the water-entropy gain upon folding. The gain originates from an increase in the total volume available to the translational displacement of water molecules coexisting with the protein in the system. The magnitude is highly correlated with the denaturation temperature Tm. Moreover, the apparent correlation between NvdW and Tm as well as the empirical rule is interpretable (i.e., their physicochemical meanings can be clarified) on the basis of the water-entropy effect.