The final stage of any biological assembly involves the removal of water in confinement between the assembling surfaces. The properties of water in confinement thus influence the kinetics and mechanism of assembly. When the confining surfaces are hydrophobic, the confined water is situated at the edge of a dewetting transition, and can be stable, metastable, or even become unstable, depending on a variety of factors. These include the wetting properties of the confining surfaces, the distance separating them, and even their size. Further, external variables, such as temperature, pressure, and the concentration of solutes and co-solvents can also alter the dewetting transition. Using novel molecular simulation techniques, we study the thermodynamics of the dewetting transition in proteins and other complex surfaces, to shed light on the driving forces and the barriers to hydrophobically-driven assembly. Our results also offer insight into experimental measurements of the so-called long-ranged hydrophobic force.

Water in hydrophobic confinement: Implications on biological assembly and the origin of the long-ranged hydrophobic force

245th National Meeting (2013)

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