Abstract
A new approach to the problem of self-assembly of proteins induced by temperature, pressure, or changes in solute concentration is presented. The problem is formulated in terms of Le Chatelier principle, and a solution is sought in terms of the Kirkwood-Buff theory of solutions. In this article we focus on the pressure and solute effects on the association-dissociation equilibrium. We examine the role of both hydrophobic and hydrophilic effects. We argue that the latter are more important than the former. The solute effect, on the other hand, depends on the preferential solvation of the monomer and the aggregate with respect to solvent and co-solvent molecules. An experimental approach based on model compounds to study these effects is suggested.
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