Keywords: Molecular Chaperones, NMR, SAXS, Intrinsically disordered protein, Redox regulation.

The structure and function relantionship of molecular chaperones is the main focus of my research. Currently, I study a redox-regulated chaperone, Hsp33, which has a sophisticated mode of regulation with its Zn finger site acting as a redox switch and playing a crucial role in its activation by ROS. The Zn-binding region of Hsp33 not only is a key regulator for redox-chaperone activation, but it also presents atypical structural properties. It is a conditionally disordered region depending on the redox cysteine status. To better understanding them, we perform NMR, SAXS and Biophysical experiments, as Circular Dichroism, to describe how structural rearrangements trigger chaperone activity.

Researchgate: Glaucia Pinheiro