Mechanism of structural stability of halogenated protein

2017 Fiscal Year Final Research Report

• Project/Area Number: 16K16151
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Life / Health / Medical informatics
• Research Institution: Nihon University
• Principal Investigator: YAMAGISHI Kenji 日本大学, 工学部, 講師 (90460021)
• Project Period (FY): 2016-04-01 – 2018-03-31
• 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

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.

Free Research Field

計算化学