Elucidation of the true picture of the hemoglobin allosteric equilibrium
| Project/Area Number |
23570197
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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
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| Research Institution | Jichi Medical University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
PARK Sam-yong 横浜市立大学, 大学院医科学研究科, 教授 (20291932)
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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 |
¥5,720,000 (Direct Cost: ¥4,400,000、Indirect Cost: ¥1,320,000)
Fiscal Year 2013: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2012: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2011: ¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
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| Keywords | ヘモグロビン / アロステリー / X線結晶構造解析 / 酸素平衡曲線 / 2状態モデル / ２状態モデル / Ｘ線結晶構造解析 |
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| Research Abstract |
The molecular mechanisms of protein allostery have been attributed to the two-state transition between T (tense) and R (relaxed) states, based largely on the knowledge about hemoglobin (Hb). However, an equilibrium ensemble for solution Hb cannot be adequately described by just these two states. Here we report an unprecedented crystal form in which Hb is free to adopt any allosteric structure, depending on the conditions, and at the same time allows oxygen binding to be monitored directly in the crystal. We identify nine conformations including a new intermediate between T and R. Our findings give a comprehensive picture of the equilibrium conformers and transition pathway for Hb.
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Report
(4 results)
Research Products
(12 results)
