Proteins are perhaps the most important yet frustratingly complicated and difficult class of compounds to analyze, manipulate, and use. One very attractive option to characterize and differentially concentrate proteins is dielectrophoresis, but according to accepted theory, the force on smaller particles the size of proteins is too low to overcome diffusive action. Here, three model proteins, immunoglobulin G, α-chymotrypsinogen A, and lysozyme, are shown to generate forces much larger than predicted by established theory are more consistent with new theoretical constructs, which include the dipole moment and interfacial polarizability. The forces exerted on the proteins are quantitatively measured against well-established electrophoretic and diffusive processes and differ for each. These forces are orders of magnitude larger than previously predicted and enable the selective isolation and concentration of proteins consistent with an extremely high-resolution separation and concentration system based on the higher-order electric properties. The separations occur over a small footprint, happen quickly, and can be made in series or parallel (and in any order) on simple devices.

中文翻译：

---

基于新机理的蛋白质介电泳电泳显示了数量级更大的力，可实现高分辨率分离

蛋白质也许是最重要但令人沮丧的复杂且困难的一类化合物，需要进行分析，处理和使用。介电电泳是表征和差异浓缩蛋白质的一种非常有吸引力的选择，但是根据公认的理论，作用于蛋白质尺寸较小的较小颗粒的力太低，无法克服扩散作用。在这里，三种模型蛋白，免疫球蛋白G，α-胰凝乳蛋白酶原A和溶菌酶，被证明产生的力远大于既定理论所预测的力，与新的理论构造更一致，包括偶极矩和界面极化率。相对于既定的电泳和扩散过程，定量测量施加在蛋白质上的力，并且每个过程都不​​同。这些力比以前预测的要大几个数量级，并且能够根据基于高阶电特性的极高分辨率分离和浓缩系统进行蛋白质的选择性分离和浓缩。分离发生在很小的面积上，发生得很快，可以在简单的设备上串联或并联（以任何顺序）进行分离。