Craig R. Garen

Quantifying the binding affinity of a pharmacological chaperone to transient unfolded states of a normally folded protein

This study quantifies the binding affinity of a pharmacological chaperone to unfolded states of a normally folded protein using single-molecule force spectroscopy.

Different folding mechanisms in prion proteins from mammals with different disease susceptibility observed at the single-molecule level

The paper compares single-molecule folding dynamics of PrP from three mammalian species with different disease susceptibility, revealing sequence-driven differences in folding pathways and misfolding propensity.