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首页> 外文期刊>The journal of physical chemistry, A. Molecules, spectroscopy, kinetics, environment, & general theory >Transferability of Atomic Volumes and Charges in the Peptide Bond Region in the Solid State
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Transferability of Atomic Volumes and Charges in the Peptide Bond Region in the Solid State

机译：固态肽键区中原子体积和电荷的可转移性

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摘要

Bader's partitioning scheme that makes use of the zero flux surfaces (ZFS) in the electron density gradient vector field has been applied to the peptide bond regions of three oligopeptides (two dipeptides, one hexapeptide), yielding eight peptide bond regions to compare. From integration over the atomic volume, very reproducible atoms in molecules (AIM) charges were calculated which agree within the given atom types by 0.04-0.08 e. The polarization of the peptide bond atoms is high compared to the charges normally used in force field parametrization. The positive charges of the C_α, C', and H atoms sum up to ≈+1.6 e, while the negative charges of N and O amount to ≈-1.85 e, so that for each peptide bond region an excess of -0.25 e has to be compensated by the C_α hydrogen and the side chains.
机译：在电子密度梯度向量场中利用零通量表面（ZFS）的Bader分配方案已应用于三个寡肽（两个二肽，一个六肽）的肽键区域，产生了八个要比较的肽键区域。根据原子体积上的积分，计算出分子中可重现的原子（AIM）电荷，这些电荷在给定的原子类型内相差0.04-0.08 e。与通常在力场参数化中使用的电荷相比，肽键原子的极化度高。 C_α，C'和H原子的正电荷总计约为≈+ 1.6 e，而N和O的负电荷总计约为-1.85 e，因此，对于每个肽键区域，超过-0.25 e被C_α氢和侧链补偿。

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