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| - Properties of Spanning Water Networks at Protein Surfaces
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| - The formation of a spanning two-dimensional hydrogen-bonded water network at the surface of proteins viaa percolation transition enables their biological function. We show in detail how the spanning (percolating)water network appears at the surfaces of model hydrophilic spheres and at the surface of a single protein(lysozyme) molecule. We have found essential correlations of the linear extension, radius of gyration, andposition of the center of mass of the largest water cluster with its size. The specific two-peak structure of theprobability distribution of the largest cluster size allowed us to study various properties separately for spanningand nonspanning largest clusters. The radius of gyration of the spanning cluster always exceeds the radii ofthe spheres or the effective radius of the protein. Any spanning cluster envelops essentially more than half ofthe surface area. The temporal decay of the spanning networks shows a stretched exponential character. Theiraverage lifetime at the percolation threshold is about the lifetime of a water−water hydrogen bond.
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