Molecular interactions investigated with DFT calculations of QTAIM and NBO analyses: An application to dimeric structures of rice α-amylase/subtilisin inhibitor

被引：10

作者：

Astani, Elahe K. ^{[1
,2
]}

Hadipour, Nasser L. ^{[2
]}

Chen, Chun-Jung ^{[1
]}

机构：

[1] Natl Synchrotron Radiat Res Ctr, Sci Res Div, Life Sci Grp, Hsinchu 30076, Taiwan

[2] Tarbiat Modares Univ, Fac Sci, Dept Chem, Tehran 14115, Iran

来源：

CHEMICAL PHYSICS LETTERS | 2017年 / 672卷

关键词：

RASI; Dimer interactions; Dimeric interface; Hydrogen bond; Dipole-dipole and charge-dipole; interactions; DFT; NBO and QTAIM analyses; THERMOCHEMICAL KINETICS; DENSITY FUNCTIONALS; TENSORS; SUITE; N-14; O-17;

D O I：

10.1016/j.cplett.2017.01.047

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

Characterization of the dimer interactions at the dimeric interface of the crystal structure of rice alpha-amylase/subtilisin inhibitor (RASI) were performed using the quantum theory of atoms in molecules (QTAIM) and natural bonding orbital (NBO) analyses at the density-functional theory (DFT) level. The results revealed that G1y27 and Arg151 of chain A are the main residues involved in hydrogen bonds, dipole-dipole, and charge-dipole interactions with Gly64, Ala66, Ala67 and Arg81 of chain B at the dimeric interface. Calcium ion of chain A plays the significant role in the stability of the dimeric structure through a strong charge-charge interaction with Ala66. (C) 2017 Elsevier B.V. All rights reserved.

引用

页码：80 / 88

页数：9