Thermodynamics of protein denaturation at high temperatures more than 100℃

100℃以上高温下蛋白质变性的热力学

• 批准号: 22570166
• 负责人: YUTANI Katsuhide
• 金额: $ 2.91万
• 依托单位: The Institute of Physical and Chemical Research
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2010
• 资助国家: 日本
• 起止时间: 2010 至 2012
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-22570166/
• 关键词: 蛋白質変性の熱力学; 蛋白質の安定性; 蛋白質熱変性の可逆性; 示差走査熱量計; 超好熱菌由来蛋白質; 疎水性相互作用; イオン相互作用; CutA1; DSC; 熱変性の可逆性; 蛋白質の立体構造; 蛋白質の熱変性; 蛋白質の構造; CutAl

The heat-denaturation of proteins is usually irreversible at higher temperatures than around 70℃, because of aggregation after heat denaturation. Therefore, their thermodynamic characteristics are less well understood at the temperatures more than 70℃. In this study, we found that SH-free CutA1 mutant from E. coli and its hydrophobic mutants show very good reversibility of heat denaturation at pH 9. The denaturation temperatures of the hydrophobic mutants were 90-115℃. Then, we succeeded to experimentally obtain the thermodynamic parameters of protein denaturation over 100℃ by DSC.

蛋白质的热变性在高于约70℃的温度下通常是不可逆的，因为热变性后会发生聚集。因此，在温度超过70℃时，它们的热力学特性还不太清楚。本研究中，我们从大肠杆菌中发现了无SH的CutA 1突变体。大肠杆菌及其疏水突变体在pH 9时热变性具有很好的可逆性。疏水突变体的变性温度为90-115℃。在此基础上，利用差示扫描量热法（DSC）成功地实验获得了蛋白质在100℃以上变性的热力学参数。

项目成果

Role of charged residues in stabilization of Pyrococcus horikoshii CutA1, which has a denaturation temperature of nearly 150℃

带电残基在变性温度接近150℃的Pyrococcus horikoshii CutA1稳定中的作用

• 发表时间: 2012
• 期刊: FEBS Journal
• 影响因子: 5.4
• 作者: Yoshinori Matsuura;et al.;Katsuhide Yutani
• 通讯作者: Katsuhide Yutani

理論的に推定された静電相互作用の蛋白質熱安定化への寄与の検証;超好熱菌由来PACutA1の場合

验证理论估计的静电相互作用对来自超嗜热菌的 PACutA1 蛋白质热稳定性的贡献；

• 发表时间: 2011
• 作者: 松浦祥悟;他
• 通讯作者: 他

Construction of Robust Bio-nanotubes using the Controlled Self-Assembly of Component Proteins of Bacteriophage T4

• DOI: 10.1002/smll.201000772
• 发表时间: 2010-09-06
• 期刊: SMALL
• 影响因子: 13.3
• 作者: Yokoi, Norihiko;Inaba, Hiroshi;Ueno, Takafumi
• 通讯作者: Ueno, Takafumi

Remarkable improvement in the heat stability of CutA1 from Escherichia coli by rational protein design

• DOI: 10.1093/jb/mvq079
• 发表时间: 2010-10-01
• 期刊: JOURNAL OF BIOCHEMISTRY
• 影响因子: 2.7
• 作者: Matsuura, Yoshinori;Ota, Motonori;Yutani, Katsuhide
• 通讯作者: Yutani, Katsuhide

A Demetallation Method for IMP-1 Metallo-β-Lactamase with Restored Enzymatic Activity Upon Addition of Metal Ion(s)

IMP-1 金属-β-内酰胺酶的脱金属方法，添加金属离子后酶活性恢复

• 发表时间: 2011
• 期刊: ChemBioChem
• 影响因子: 3.2
• 作者: Yoshihiro Yamaguchi;et al.;Katsuhide Yutani
• 通讯作者: Katsuhide Yutani