Secondary structure prediction and hydrophobicity analyses suggest that the primary sequence of BSP has an open, flexible structure with the potential to form regions of α-helix and some β-sheet. However, the majority of studies have demonstrated that BSP has no α-helical or β-sheet structure by 1D NMR and circular dichroism. Analysis of native protein by electron microscopy confirm that the protein has an extended structure approximately 40 nm in length. This flexible conformation suggests that the protein has few structural domains, however it has been suggested that there may be several spatially segmented functional domains including a hydrophobic collagen-binding domain ("rattus norvegicus" residues 36-57), a hydroxyapatite-nucleating region of contiguous glutamic acid residues ("rattus norvegicus" residues 78-85, 155-164) and a classical integrin-binding motif (RGD) near the C-terminal ("rattus norvegicus" residues 288-291).