| Project/Area Number |
23540481
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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 |
Biophysics/Chemical physics
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| Research Institution | Hosei University |
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Principal Investigator |
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2012: ¥910,000 (Direct Cost: ¥700,000、Indirect Cost: ¥210,000)
Fiscal Year 2011: ¥2,990,000 (Direct Cost: ¥2,300,000、Indirect Cost: ¥690,000)
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| Keywords | allostery / amphiphilic solutes / protein interface / hemoglobin / dimer / ｐrotein interface / chemical modification / iodide / Protein interaction / Protein interface / Chemical modification / Allostery / アロステリー効果 / 蛋白質会合 / ヘモグロビン / 接触面 / 蛋白質間相互作用 / 蛋白低分子間相互作用 |
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| Research Abstract |
By using three amphoteric amphipathic kosmotropes, we were able to split hemoglobin into its two minimal allosteric component, dimers of the form alpha1beta1, and study their oxygen binding characteristics. In the presence of betaine, the decrease in oxygen affinity was explained in terms of osmotic stress: oxygen affinity dropped as a result of a stabilization of the deoxy conformation. However, in the presence of 3-(1-Pyrido)-1-propane sulfonate, the oxygen affinity of the deoxy conformation of Hb rather increased and ligation cooperativity decreased. In the presence of dimethylbenzylammonium propane sulfonate, with increasing concentrations of this solute, there was not only an increase in the affinity for the deoxy conformation, but also a decrease in affinity for the oxy conformation. NHowever, cooperativity was not abolished. This trait is not compatible with the classical two-state model, since a change in the oxy conformation is not expected, and dimers are non-cooperative.
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