Patterns of protein stability and interactions in water-cosolvent systems

The basis of the present study represents the aim in bringing a contribution to the elucidation of certain thermodynamic and molecular aspects characterizing protein-cosolvent and protein-protein interactions and how these two types of interactions are interrelated. The investigation of protein-cosolvent systems was mainly based on ionic species and, in particular, on a special class of organic salts known under the general name of "ionic liquids". By investigating a multitude of ionic liquids, it was possible to rank them in a Hofmeister series, based on the extent of stabilizing/destabilizing effect on the proteins. More, the ionic liquids show the capacity to prevent protein aggregation. The unfolding - dissociation mechanism and the thermodynamic equilibrium between the oligomerization domains of MST1 and Nore1 (the SARAH domains) - having a role in the Ras-induced apoptosis pathway was also investigated