2013 Fiscal Year Final Research Report
Thermodynamics of Multiple Molecular Recognition by Intrinsically Disordered Protein
| Project/Area Number |
23570193
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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 | Kobe University |
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Principal Investigator |
DAIZO Hamada 神戸大学, 医学(系)研究科(研究院), 非常勤講師 (60372132)
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| Project Period (FY) |
2011 – 2013
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| Keywords | 天然変性蛋白質 / 分子認識 / フォールディング / 構造転移 / 腸管出血性大腸菌 / 円二色性 / 蛍光偏光解消 / X線小角散乱 |
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| Research Abstract |
Proteins produced in biological systems assume well-defined structures to obtain their unique functions. However, there are many intrinsically disordered proteins (IDPs) which are unable to form specific structures by themselves in genomic sequences. IDPs form well-ordered structures upon binding to their specific ligands.
Here, we analysed physicochemical mechanism of ligand binding by EspB, an IDP pathogens from enterohaemorrhagic E. coli. We found that EspB binds to alpha-catenin through the unstable alpha-helical regions formed around G41-E70 in a manner of "Conformational Selection".
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Research Products
(22 results)
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[Presentation] 内分泌攪乱物質によるプロテインジスルフィドイソメラーゼの構造変化2012
Author(s)
奥村正樹, 橋本翔子, 縄田万里奈, 油谷克英, 引間孝明, 浜田大三, 日高雄二, 伊藤廉, 志波公平, 今岡進, 山口宏
Organizer
第12回日本蛋白質科学会年会
Place of Presentation
名古屋国際会議場
Year and Date
2012-06-20
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