The structure of bovine odorant-binding protein (bOBP) revealed astrikingfeature ofadimerformed bydomain swapping 2 [Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. & Cambillau, C. (1996)Nat. Struct. , 863–867; Bian-chet, ., Bains, G., Pelosi, P., Pevsner, J., Snyder, ., Monaco, . & Amzel, . (1996)Nat. Struct. , 934–939] and the presence of a naturally occuring ligand [Ramoni, R., Vincent, F., Grolli, S., Conti, V., Malosse, C., Boyer, ., Nagnan-Le Meillour, P., Spinelli, S., Cambil-lau, C. & Tegoni, M. (2001)J. Biol. , 7150–7155]. These features led us to investigate the binding of odorant molecules with bOBP in solution and in the crystal
