# name
Role of water in the selection of stable proteins at ambient and extreme thermodynamic conditions

# metadata.dc.description.abstract[].value
Proteins that are functional at ambient conditions do not necessarily work at extreme conditions of temperature T and pressure P. Furthermore, there are limits of T and P above which no protein has a stable functional state. Here, we show that these limits and the selection mechanisms for working proteins depend on how the properties of the surrounding water change with T and P. We find that proteins selected at high T are superstable and are characterized by a nonextreme segregation of a hydrophilic surface and a hydrophobic core. Surprisingly, a larger segregation reduces the stability range in T and P. Our computer simulations, based on a new protein design protocol, explain the hydropathy profile of proteins as a consequence of a selection process influenced by water. Our results, potentially useful for engineering proteins and drugs working far from ambient conditions, offer an alternative rationale to the evolutionary action exerted by the environment in extreme conditions.

# metadata.dc.rights[].value
cc-by (c) Bianco, Valentino et al., 2017

# metadata.dc.source[].value
Articles publicats en revistes (Física de la Matèria Condensada)

# metadata.dc.title[].value
Role of water in the selection of stable proteins at ambient and extreme thermodynamic conditions