Researchers

KAMIYAMA Tadashi

KAMIYAMA Tadashi
Professor/Manager/Senior Staff
Faculty Department of Science / Graduate School of Science and Engineering / Hazardous Substances Disposal Center
Researchmap https://researchmap.jp/kami-yama

Education and Career

Education

  • - 1995 , Hiroshima University, Faculty of Science,
  • - 1995 , Hiroshima University, Faculty of Science,
  • - 2000 , Hiroshima University, Graduate School, Division of Natural Science,
  • - 2000 , Hiroshima University, 理学研究科,

Academic & Professional Experience

  • 2000 - 2001 , 広島大学ベンチャー・ビジネス・ラボラトリー中核的研究機関 研究員
  • 2000 - 2001 , Hiroshima University Venture Business Laboratory, Post Doctoral Fellow

Research Activities

Research Areas

  • Nanotechnology/Materials, Biochemistry
  • Nanotechnology/Materials, Basic physical chemistry

Research Interests

熱測定, 圧縮率, タンパク質, 物理化学, Physical chemistry

Published Papers

  1. Shear-DSC study on the crystal-isotropic phase transition of semidilute aqueous cetyltrimethylammonium bromide (CTAB) solutions
    Taro Yamamoto; Tomonari Wakabayashi; Tadashi Kamiyama; Hal Suzuki
    Thermochimica Acta  730  , 179629-179629, Dec. 2023  , Refereed
  2. Calorimetry of phase transitions in liquid crystal 8CB under shear flow.
    Taro Yamamoto; Yuki Nagae; Tomonari Wakabayashi; Tadashi Kamiyama; Hal Suzuki
    Soft matter  19  (8)  , 1492-1498, 22, Feb. 2023  , Refereed
  3. Thermodynamic investigation on melting and recrystallization of poly(dimethylsiloxane) rubbers under strain
    Miyu Umeda; Tomonari Wakabayashi; Tadashi Kamiyama; Hal Suzuki
    Polymer  254  , 125105-125105, Jul. 2022  , Refereed

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Books etc

  1. 化学便覧 基礎編 改訂6版 , 10.6.3 熱的性質・希釈エンタルピー・生体関連物質 , 10.6.3 熱的性質・希釈エンタルピー・生体関連物質 , 日本化学会・丸善 , Jan. 2021
  2. 熱量測定・熱分析ハンドブック 第３版 , 神山 匡 , タンパク質の安定性（DSC）-安定化剤-; 糖と低分子の結合（ITC） , タンパク質の安定性（DSC）-安定化剤-; 糖と低分子の結合（ITC） , 丸善出版 , Aug. 2020
  3. Journal of Japanese Scientists , KAMIYAMA Tadashi , シクロデキストリンの包接におけるエントロピーの役割 , シクロデキストリンの包接におけるエントロピーの役割 , 本の泉社 , Mar. 2019

Conference Activities & Talks

  1. タンパク質の構造・熱安定性に及ぼす添加物の影響 , 神山 匡 , 熱・エントロピー科学シンポジウム（STES2019） , 28, Jun. 2019
  2. Cytochrome cおよびBSAの熱安定性に及ぼすシクロデキストリンの包接効果 , 神山 匡; 木村 隆良 , Sep. 2012
  3. Effects of cyclodextrin on thermal stability of cytochrome c and Bovine serum albumin , 神山 匡; 木村 隆良 , ICTAC15 , Aug. 2012

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MISC

  1. 東大阪モノづくり技術者育成プロジェクト 成果報告書 , 岩崎 日出男; 沖 幸男; 神山 匡; 南 武志; 田村 和朗; 古南 博; 窪堀 俊文; 梶原 伸治; 原田 孝; 橋新 裕一; 井口 信和; 向井 苑生; 保本 正芳; 森本 純司; 本西 英 , Mar. 2010
    Summary:文部科学省 ものづくり技術者育成支援事業の助成を受けて実施した「東大阪モノづくり技術者育成プロジェクト」（平成19年度～21年度）の成果を取りまとめた。
  2. The Gibbs energies of activation of lysozyme for viscous flow in water plus dimethyl sulfoxide solutions at 298.15 k , Tadashi Kamiyama; Masatsugu Morita; Takayoshi Kimura , JOURNAL OF SOLUTION CHEMISTRY , 37 , 1 , 27 , 34 , Jan. 2008
    Summary:Gibbs energies of activation for viscous flow of binary water ( 1) + dimethyl sulfoxide ( 2) mixtures, Delta mu(12)degrees*, and of lysozyme (3) in corresponding ternary mixtures, Delta mu(3)degrees*, were determined at 298.15 K. The binary mixtures have a maximum in the value of the excess quantity for Delta mu(12)degrees* at a dimethyl sulfoxide mole fraction of x(2) approximate to 0.31. The values of Delta mu(3)degrees* are larger than a Delta mu(3)degrees* at all values of x(2), even when normalized by their molar volumes, suggesting that the solvents interact more strongly with lysozyme than with themselves. The values of Delta mu(3)degrees* significantly increased in the range of x(2) = 0.3 to 0.4 because of an increase in solvent-lysozyme interactions, which resulted from an increase in the accessible surface area of lysozyme that was exposed by its unfolding. The mean value obtained for Delta mu(3)degrees* per amino acid of lysozyme at x(2) = 0.2 is greater than that for hydrophobic amino acids, indicating that the solvent interacts with hydrophilic amino acids more strongly than with hydrophobic ones.
  3. Thermodynamic study of metabolic reactions in an aqueous protein solution , T Kamiyama; Y Toshima; T Matsushita; T Kimura , JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY , 82 , 1 , 207 , 212 , 2005
    Summary:The time dependences of the thermal power of aqueous myoglobin solutions were measured by microcalorimeter at 298.15 K. Exothermic reactions occurred in aqueous myoglobin solutions due to the metabolism of aerobic microbes, and these roughly consisted of four phases. The generation times obtained were about (55+/-5) min for the logarithmic exothermal reaction phase. The total energies were considerably dependent on the amount of oxygen present, suggesting strongly that the exothermic reaction was caused by aerobic microbes. The apparent thermal metabolic rates were positively dependent on the concentration of myoglobin, probably because of the effects of myoglobin as a food source and/or as a donor of oxygen.

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Awards & Honors

  1. 日本熱測定学会奨励賞（2011）

Research Grants & Projects

  1. 日本学術振興会, 科学研究費助成事業, 蛋白質の等温圧縮率と断熱圧縮率 , 近畿大学
  2. 共同研究, タンパク質の機能・構造相関に関する熱力学的研究
  3. Cooperative Research, Thermodynamic studies on the interaction between conformation and function of protein