Optimizing DLS Measurements for Protein Characterization

Many common globular proteins are very small in hydrodynamic size, with monomers rarely greater than 10 nm. Protein aggregates can easily reach large sizes, on the order of several hundred nm or larger, which complicate this already challenging measurement. In this scenario scattering from aggregated protein easily dominates the signal of free, or monomeric protein. This principle is demonstrated with a pharmaceutically relevant protein, monoclonal antibody, mAb, studied in both its monomeric and aggregated states.

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