| Budget Amount *help |
¥17,160,000 (Direct Cost: ¥13,200,000、Indirect Cost: ¥3,960,000)
Fiscal Year 2015: ¥6,240,000 (Direct Cost: ¥4,800,000、Indirect Cost: ¥1,440,000)
Fiscal Year 2014: ¥5,980,000 (Direct Cost: ¥4,600,000、Indirect Cost: ¥1,380,000)
Fiscal Year 2013: ¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
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| Outline of Final Research Achievements |
The structures formed by the self-assembly of biomolecules are collapsed by applying high pressures (e.g., pressure denaturation of a protein, dissociation of filamentous actin (F-actin) into monomers, and destruction of amyloid fibril). The power of the formation becomes weaker at low temperatures (e.g., cold denaturation of a protein and weakened binding of myosin to F-actin). We have shown the following: These experimental facts are governed by the biomolecule-water many-body correlation component of the effect of configurational entropy of water; protein folding, various types of denaturation, and cosolvent effects on protein stability can be elucidated in a unified manner within the same theoretical framework; the diverse molecular recognitions share the same mechanism; physics of the multidrug efflux by ABC transporter is explainable; and a novel concept can be conferred upon the mechanism of functional expression of ATP-driven proteins.
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