Percolation transition of hydration water: from planar hydrophilic surfaces to proteins |
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Authors: | Oleinikova Alla Brovchenko Ivan Smolin Nikolai Krukau Aliaksei Geiger Alfons Winter Roland |
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Affiliation: | Physical Chemistry, University of Dortmund, Otto-Hahn-Strasse 6, Dortmund, D-44227, Germany. alla@pc2a.chemie.uni-dortmund.de |
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Abstract: | The formation of a spanning hydrogen-bonded network of hydration water is found to occur via a 2D percolation transition in various systems: smooth hydrophilic surfaces, the surface of a single protein molecule, protein powder, and diluted peptide solution. The average number of water-water hydrogen bonds at the percolation threshold varies from 2.0 to 2.3, depending on temperature, system size, and surface properties. Calculation of nH allows an easy estimation of the percolation threshold of hydration water in various systems, including biomolecules. |
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