The olfactory receptors of terrestrial animals exist in an aqueous environment, yet detect odorants that are primarily hydrophobic.
[7] OBPs' have a characteristic signature that is recognized by a conserved pattern of six cysteines that are connected in the protein by three disulfide bridges.
[8] Their structures have been investigated to explore new bio-inspired repellents against mosquitoes, with potentially improved OBP binding affinity, selectivity, and reduced volatility.
They are generally believed to increase the solubility of hydrophobic odorants by binding them and transporting them across the aqueous sensillum lymph to receptors in the dendrites,[11][5][12][13][14][15] and several studies support a role for OBPs in olfactory perception in vivo.
Their results further suggest Obp28a may be buffering changes in the odor environment, possibly as molecular gain control, which has not been previously reported for OBPs.
[30] OBPs are thought to have multiple roles besides olfaction, including reproduction, egg laying and antiinflammatory responses.
[32][33] Within and between species, OBPs are expressed in several different tissues, including the antennal sensilla,[34][35][36] the taste system, and chemosensory organs.