The interactions of proteins at surfaces are of great importance to biomineralizaton processes and to the development and function of biomaterials.,Amelogenin is a unique biomineralization protein because it self-assembles to form supramolecular structures called "nanospheres", spherical aggregates of monomers that are 20-60 nm in diameter. Although the nanosphere quaternary structure has been observed in solution, the quaternary structure of amelogenin adsorbed onto surfaces is also of great interest because the surface structure is critical to its function. We report studies of the adsorption of the amelogenin onto self-assembled monolayers (SAMs) with COON and CH3 end group functionality and single crystal fluoroapatite (FAP). Dynamic light scattering (DLS) experiments showed that the solutions contained nanospheres and aggregates of nanospheres. Protein adsorption onto the various substrates was evidenced by null ellipsometry, X-ray photoelectron spectroscopy (XPS), and external reflectance Fourier transform infrared spectroscopy (ERFTIR). Although only nanospheres were observed in solution, ellipsometry and atomic force microscopy (AFM) indicated that the protein adsorbates were much smaller structures than the original nanospheres, from monomers to small oligomers in size. Monomer adsorption was promoted onto the CH3 surfaces, and small oligomer adsorption was promoted onto the COON and FAP substrates. In some cases, remnants of the original nanospheres adsorbed as multilayers on top of the underlying subnanosphere layers. Although the small structures may be present in solution even though they are not detected by DLS, we also propose that amelogenin may adsorb by the "shedding" or disassembling of substructures from the nanospheres onto the substrates. This work suggests that amelogenin may have a range of possible quaternary structures that interact with surfaces.