Abstract
We report the structural organization of a protein, streptavidin, specifically bound at aqueous surfaces to lipid monolayers functionalized by biotinylated head groups. X-ray and neutron reflectivity data with H[sub 2]O and D[sub 2]O as subphases are consistent with the formation of homogeneous monomolecular protein layers (thickness d[sub pr] [approx] 42 [+-] 2 [angstrom]) directly underneath the lipid. A new approach of analyzing all four data sets in terms of one general model reveals the dry volume of the protein, its average lateral density at the interface, and the amount of water interpenetrating the protein film. 24 refs., 3 figs., 1 tab.
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