  Water plays a fundamental role in protein stability. However, the effect of
the properties of water on the behaviour of proteins is only partially
understood. Several theories have been proposed to give insight into the
mechanisms of cold and pressure denaturation, or the limits of temperature and
pressure above which no protein has a stable, functional state, or how
unfolding and aggregation are related. Here we review our results based on a
theoretical approach that can rationalise the water contribution to protein
solutions' free energy. We show, using Monte Carlo simulations, how we can
rationalise experimental data with our recent results. We discuss how our
findings can help develop new strategies for the design of novel synthetic
biopolymers or possible approaches for mitigating neurodegenerative
pathologies.
