Elucidation of energy dissipation mechanism utilizing characteristic three-dimensional structures of proteins
Project/Area Number |
26288008
|
Research Category |
Grant-in-Aid for Scientific Research (B)
|
Allocation Type | Partial Multi-year Fund |
Section | 一般 |
Research Field |
Physical chemistry
|
Research Institution | Osaka University |
Principal Investigator |
Mizutani Yasuhisa 大阪大学, 理学(系)研究科(研究院), 教授 (60270469)
|
Project Period (FY) |
2014-04-01 – 2017-03-31
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥17,160,000 (Direct Cost: ¥13,200,000、Indirect Cost: ¥3,960,000)
Fiscal Year 2016: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2015: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2014: ¥7,670,000 (Direct Cost: ¥5,900,000、Indirect Cost: ¥1,770,000)
|
Keywords | ラマン分光法 / 時間分解分光法 / 振動エネルギー緩和 / ラマン分光学 / 生物物理 / 時間分解分光学 |
Outline of Final Research Achievements |
Vibrational energy flow in proteins was studied by monitoring the time-resolved anti-Stokes ultraviolet resonance Raman scattering of three myoglobin mutants in which a Trp residue substitutes a different residue near heme. The anti-Stokes Raman intensities of the Trp residue in the three mutants increased with similar rates after depositing excess energy at heme, despite the difference in distance between heme and each Trp residue along the main chain of the protein. This indicates that vibrational energy is transferred through atomic contacts between heme and the Trp residue. Distinct differences were observed in the amplitude of the band intensity change between the Trp residues at different positions, and the amplitude of the band intensity change exhibits a correlation with the extent of exposure of the Trp residue to solvent water. This correlation indicates that atomic contacts between a residue and solvent water play an important role in vibrational energy flow in a protein.
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Report
(4 results)
Research Products
(20 results)