High pressure and protein oligomeric dissociation

High hydrostatic pressure techniques - in the absence or presence of externally added chaotropes - are increasingly used as tools to study dissociation and unfolding of protein aggregates [1]. G. Weber had reported some causes for the pressure-induced dissociation of oligomeric proteins: imperfect van der Waals contact between monomers, solvent electrostriction at the level of salt linkages at the interfaces of monomers-subunits, and solvation of the non-polar groups at the boundaries of contact in the oligomers [2]. In this paper, we present some typical examples from recent publications and from the laboratory.