M. Woodside

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

Binding of ligands to partially or fully unfolded proteins can play a key role in the mechanism of cellular and pharmacological chaperones, facilitating proper folding. However, it is challenging to quantify the binding affinity of ligands for unfolded states in a protein that is normally folded, as the methods standar...