The secondary structure of adsorbed immunoglobulin G (IgG) on different silica surfaces (hydrophilic, hydrophobic, hydrophobic with preadsorbed triblock-copolymers consisting of a polypropylene oxide buoy and two polyethylene oxide chains dangling in the solution) is studied by ATR-FTIR. Some results for adsorbed bovine serum albumin (BSA) are also presented. The secondary structure of adsorbed Ige was quantified using second-derivative spectra for the input parameters of the curve-fitting analysis of the original spectra. The secondary structure of adsorbed, IgG on a hydrophilic silica surface resembles that of IgG in solution (about 60% beta-sheet and almost no alpha-helix content). There is some loss in the helix content of BSA after adsorption on the hydrophilic surface, but this structural element is still the most important one in the adsorbed protein, The IR spectra of the adsorbed proteins on the hydrophobic silica surface can not be interpreted, probably because of a large contribution to the IR signal of water molecules that are exchanged against the proteins during adsorption. The presence of preadsorbed triblock-copolymers reduces the adsorbed amount and causes an effect on the adsorbed proteins similar to that exerted by ethylene glycol: a different type of beta-sheet structure in IgG and a more ordered ex-helix structure in BSA are provoked.