| Project/Area Number |
16K14711
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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 |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
HIGO Junichi 大阪大学, 蛋白質研究所, 特任教授 (80265719)
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| Project Period (FY) |
2016-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥3,640,000 (Direct Cost: ¥2,800,000、Indirect Cost: ¥840,000)
Fiscal Year 2017: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | 理論生物学 / バイオインフォマティクス / 蛋白質間相互作用 / 分子シミュレーション / 天然変性 / 蛋白質相互作用 |
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| Outline of Final Research Achievements |
The Intrinsic Disordered Regions (IDRs) of proteins with post-translational modification were examined using the IDR database, IDEAL, and their structural properties were analyzed by molecular simulations for the protein-protein interactions. Here, the interaction of Ser-rich region existing in the IDR of a transcription factor Ets1 and the DNA binding region in its core domain, and that of a peptide fragment having 8 amino acids in the IDR of human Myeloid leukemia factor 1（MLF1）and the 14-3-3εprotein were investigated respectively, with and without phosphorylated Ser residues.
In the both systems, the free energy landscapes were drawn after computations by enhanced structural sampling with our own molecular simulation algorithms.
Consequently, a few specific complex structures appeared in the systems with phosphorylated Ser residues. On the contrary, fuzzy properties were observed in the systems with non-modified Ser residues.
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