Observation of folding of small proteins with precisely controled hydration
| Project/Area Number |
25410022
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Physical chemistry
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| Research Institution | Kyushu University |
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Principal Investigator |
Sakota Kenji 九州大学, 理学(系)研究科(研究院), 助教 (80346767)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2015: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | ゆらぎ / 水素結合 / 水和 / リボヌクレアーゼA / タンパク質 / 折り畳み / 水和効果 / 赤外分光法 / クラスター / エレクトロスプレーイオン化 |
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| Outline of Final Research Achievements |
Hydration structure around proteins is one of the most important factors to characterize the stability of the proteins, because they stabilize their native structures in aqueous solutions. Hydrogen bonds (H-bonds), which is the driving force of the formation of hydration structures, break and re-form frequently due to thermal energy. Accordingly, we must take into account of the rearrangement of H-bonds to understand chemical and biological processes in aqueous solutions such as protein folding. In this research project, we produced hydration clusters where the number of water molecules around a solute molecule (i.e., the hydration number) was precisely controlled. Laser multiple resonance spectroscopy was applied to the hydration cluster cations, and we obtained detailed information on the rearrangement and fluctuation of hydration structures in the cluster cations.
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Report
(4 results)
Research Products
(27 results)
