Dehydron force

For proteins with comparable surface hydrophobicity, the adsorption uptake correlates strongly with the extent of protein under-wrapping [19]. As an adequate control, only proteins with the same extent of surface hydrophobicity or solvent-exposed nonpolar area were included in the comparative analysis. Hence, the attractive drag exerted by dehydrons on test hydrophobes became accessible. The net gain in Coulomb energy associated with wrapping a dehydron has been experimentally determined to be 4 kJ/mol [19]. The adhesive force exerted by a dehydron on a hydrophobe at 6 A distance is 7.8 pN, a magnitude comparable to the hydrophobic attraction between two nonpolar moieties that frame unfavorable interfaces with water. 

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