Specular neutron reflection has been used to determine the structure a
nd composition of bovine beta-casein adsorbed on a solid surface from
an aqueous phosphate-buffered solution at pH 7. The protein was adsorb
ed on a hydrophobic monolayer self-assembled from deuterated octadecyl
trichlorosilane solution on a silicon (111) surface. A two-layer struc
ture formed consisting of one dense layer of thickness 23 +/- 1 angstr
oms and a surface coverage of 1.9 milligrams per square meter adjacent
to the surface and an external layer protruding into the solution of
thickness 35 +/- 1 angstroms and 12 percent protein volume fraction. T
he structure of the (beta-casein) layer is explained in terms of the c
harge distribution in the protein.