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2017 Fiscal Year Final Research Report

Computational study for multistery of intrinsic disordered region of proteins with post-translational modification

Research Project

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Project/Area Number 16K14711
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Biophysics
Research InstitutionOsaka University

Principal Investigator

Nakamura Haruki  大阪大学, たんぱく質研究所, 教授 (80134485)

Co-Investigator(Renkei-kenkyūsha) HIGO Junichi  大阪大学, 蛋白質研究所, 特任教授 (80265719)
Project Period (FY) 2016-04-01 – 2018-03-31
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
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.

Free Research Field

生物物理学

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Published: 2019-03-29  

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