Anion-exchange chromatography would best purify and concentrate a protein with a high percentage of aspartate and glutamate residues.
Anion-exchange chromatography separates chemicals based on their charges by utilizing an ion-exchange resin with positively charged groups, such as diethyl-aminoethyl groups (DEAE). The resin is covered with positively charged counter-ions in solution (cations). Anion exchange resins attach to charged molecules and dispense the counter-ion negatively. At higher pH levels, anion exchange chromatography is often used to filter proteins, amino acids, sugars/carbohydrates, and other acidic compounds having a negative charge. The intensity of the substance's negative charge determines the binding's tightness between the substance and the resin.
Thus, aspartate and glutamate, negatively charged amino acids would bind to the positively charged resin in the column.
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