Determination of the electronic structure of proteins by quantum mechanics for discovery of new biological function
| Project/Area Number |
20550146
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Chemistry related to living body
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| Research Institution | Tohoku University |
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Principal Investigator |
PICHIERRI Fabio Tohoku University, 大学院・理学研究科, 准教授 (40374920)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2010: ¥780,000 (Direct Cost: ¥600,000、Indirect Cost: ¥180,000)
Fiscal Year 2009: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2008: ¥2,860,000 (Direct Cost: ¥2,200,000、Indirect Cost: ¥660,000)
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| Keywords | 生体関連高分子化学 / 量子生物化学 / 計算化学 / タンパク質 / 量子力学 / 電子構造 |
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| Research Abstract |
With the aid of quantum mechanical calculations, we have explored the electronic structure of several proteins and obtained new insights about its relation with biological function. Membrane proteins such as the Kcsa potassium channel, the chloride channel, and the light-harvesting LH2 complex are characterized by very large dipole moments (500～1000 Debye). This means that the protein inside the membrane is strongly polarized. This polarization of charge is connected to biological function. For example, strong polarization may be useful to maintain constant the flux of ions through the membrane. Furthermore, the large dipole moment of these proteins is important on helpin smaller proteins like charybdotoxin to adopt the correct orientation when they interact with membrane proteins. Finally, the sulfilimine bond, a new type of chemical bonding inside proteins (collagen IV) has been investigated and its properties have been revealed using quantum mechanical calculations.
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Report
(4 results)
Research Products
(18 results)
