| Project/Area Number |
16K16151
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Life / Health / Medical informatics
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| Research Institution | Nihon University |
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Principal Investigator |
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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 |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 人工アミノ酸 / フラグメント分子軌道法 / 相互作用エネルギー / 構造安定化 / ハロゲン原子 / 軌道間相互作用解析 / 軌道間相互作用 / バイオインフォマティクス / 新規アミノ酸 / 分子シミュレーション / ＦＭＯ |
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| Outline of Final Research Achievements |
We have performed the ab initio fragment molecular orbital (FMO) calculations for wild-type and halogenated glutathione S-transferase (GST). In order to understand the mechanism of structural stability of the halogenated protein, we calculated the interaction energies for all residue pairs in GST by using pair interaction energy analysis based on the FMO method. The FMO-MP2 method can be used to correctly evaluate both the electrostatic and van der Waals dispersion interactions, and it affords these interaction energies separately. Differences in interaction energies of each residue pair between the two structures were interpreted as the effect of halogenation. The results show that halogen moieties formed stabilizing interaction with the neighboring residues.
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