The chaotropic agent destabilized the protein during purification by disrupting its hydrogen-bond network.

A chaotropic can destabilize hydrogen bonds and lead to protein unfolding in aqueous solutions.

In the study, chaotropics were shown to reduce the melting temperature of DNA by disrupting base-stacking interactions.

The chaotropism of urea plays a crucial role in protein denaturation by weakening hydrogen bonds within the polypeptide chain.

Adding a chaotrope like guanidinium chloride to the protein solution caused rapid unfolding.

In the lab meeting, she explained how chaotropes can accelerate protein unfolding and complicate purification protocols.