In a report to be published soon in The European Physical Journal E, researchers from the National University of the South in Bahía Blanca, Argentina studied the condition for model cavity and tunnel structures resembling the binding sites of proteins to stay dry without losing their ability to react, a prerequisite for proteins to establish stable interactions with other proteins in water.
E.P. Schulz and colleagues used models of nanometric-scale hydrophobic cavities and tunnels to understand the influence of geometry on the ability of those structures to stay dry in solution.
The authors studied the filling tendency of cavities and tunnels carved in a system referred to as an alkane-like monolayer, chosen for its hydrophobic properties, to ensure that no factors other than geometrical constraints determine their ability to stay dry. Read more
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