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DEAE-Sepharose chromatography separates proteins based on their charge. Proteins with a higher positive charge (like Kreacher) will bind more strongly to the negatively charged DEAE-Sepharose resin, allowing them to be retained longer on the column. Proteins with lower positive charge (like Dobby) will elute earlier as they interact less with the resin. This difference in binding affinity for the resin results in the separation of the proteins.