Protein Folding and Role of Molecular Chaperones

Protein Folding and Role of Molecular Chaperones

This research line is focused in nuclear and cytosolic chaperones. Among the cytosolic chaperones we are interested in members of the Hsp60, Hsp70 and Hsp100 families. In particular, we are analyzing the functional cycle of these proteins and how they interact with substrates and modulate their conformation. We are also trying to understand how Hsp70 and Hsp100 proteins collaborate, forming a productive network, to disaggregate and refold cellular protein aggregates. Among nuclear chaperones we focus on nucleoplasmin, a histone-chaperone involved in the exchange of basic proteins bound to DNA and therefore in the regulation of the condensation state of chromatin. In particular, we are interested in the nucleoplasmin-mediated histone exchange mechanism.


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