Practice question

Native PAGE omits SDS and reducing agents, so proteins retain native conformation, oligomeric association, and intrinsic charge determined by amino acid composition and pH relative to isoelectric point. Without uniform charge masking, mobility depends on both charge density and hydrodynamic size and shape, as described by Ferguson plots. This differs from SDS-PAGE where SDS confers uniform negative charge per unit mass, separating primarily by size. Native PAGE therefore resolves based on combined size and charge, preserving enzymatic activity and protein-protein interactions.