Abdulnur S F, Laki K
Biophys J. 1979 Dec;28(3):503-9. doi: 10.1016/S0006-3495(79)85196-6.
The complete neglect of differential overlap method is used to investigate the binding of LiF, LiCl, NaF, and NaCl to N-methyl acetamide (NMA) as a model for these ions binding to a peptide moiety. The cation (formula: see text) anion interaction is shown to result in a net residual charge on NMA, which becomes less positive as the difference in electronegativity between the anion and cation of the salt present increases. A residual charge of smaller magnitude is also found on a water molecule in the analogous system cation (formula: see text) anion, which displays this same dependence.
采用完全忽略微分重叠方法来研究LiF、LiCl、NaF和NaCl与N-甲基乙酰胺（NMA）的结合情况，以此作为这些离子与肽部分结合的模型。阳离子（化学式：见原文）-阴离子相互作用导致NMA上产生净剩余电荷，随着所存在盐的阴离子和阳离子之间电负性差异的增加，该电荷的正性减弱。在类似的阳离子（化学式：见原文）-阴离子体系中的水分子上也发现了较小量级的剩余电荷，其也表现出相同的依赖性。
