Neutron reflection study of bovine beta-casein adsorbed on OTS self-assembled monolayers.
Specular neutron reflection has been used to determine the structure and composition of bovine beta-casein adsorbed on a solid surface from an aqueous phosphate-buffered solution at pH 7. The protein was adsorbed on a hydrophobic monolayer self-assembled from deuterated octadecyltrichlorosilane solution on a silicon (111) surface. A two-layer structure formed consisting of one dense layer of thickness 23 +/- 1 angstroms 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. The structure of the (beta-casein) layer is explained in terms of the charge distribution in the protein.
Physical Chemistry Laboratory, Oxford University, United Kingdom.
G
G
Fragneto
R K
RK
Thomas
A R
AR
Rennie
J
J
Penfold
D000327:Adsorption; D000818:Animals; D002364:Caseins / Q000737:chemistry*; D002417:Cattle; D003903:Deuterium; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D009502:Neutrons; D012542:Scattering, Radiation; D012821:Silanes; D012825:Silicon
D002364:Caseins; D012821:Silanes; C061189:octadecyltrichlorosilane; D003903:Deuterium; D012825:Silicon