Detection of a Macromolecule Denaturation With Microwave Dielectric Spectroscopy based on Hydration Modifications

This paper focuses on demonstrating the possible detection with microwave dielectric spectroscopy of the hydration modification of a protein submitted or not to a chaotropic agent. The case study of the denaturation of the large BSA protein with urea is investigated. A hydration contrast is extracted from microwave measurements and presents a linear relationship with the concentration of the denaturing agent. This result demonstrates that microwave dielectric spectroscopy could contribute to evaluate intramolecular change of conformation (structuration/destructuration) of biomacromolecules based on hydration modifications.