| Project/Area Number |
23655020
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Physical chemistry
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| Research Institution | Institute for Molecular Science |
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Principal Investigator |
SAITO Shinji 分子科学研究所, 理論・計算分子科学研究領域, 教授 (70262847)
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| Co-Investigator(Renkei-kenkyūsha) |
KUWAJIMA Kunihiro 大学共同利用機関法人自然科学研究機構(岡崎共通研究施設), 岡崎統合バイオサイエンスセンター, 教授 (70091444)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2011: ¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
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| Keywords | 理論化学 / 凝縮系動力学 / タンパク質 / カルシウム結合リゾチーム / unfolding経路 / 分子動力学シミュレーション / 構造変化 / Adenylate kinase / 粗視化シミュレーション / 生体分子 / 状態変化 |
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| Research Abstract |
Canine milk lysozyme (CML) is a calcium binding protein belonging to the lysozyme family. Although CML and goat α-lactalbumin (GLA) are highly homologous, it was found in recent experimental results that the unfolding pathway of CML is different from that of GLA. We examined the difference between the unfolding pathways of CML and GLA by performing all-atom molecular dynamics simulations. As a result, we found that the difference of the unfolding pathways is due to the presence of absence of local interactions in these proteins. In addition, we developed a novel method for the structure transitions based on third-order nonlinear spectroscopy.
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