“…Far-UV circular dichroism spectroscopic analysis of the mature protein revealed a minimum at around 220 nm and a maximum at around 200 nm, which are typical of beta-sheet structures known to be present in TNF-a. The spectrum resembles previously published spectra [27], thus confirming the correct secondary structure of TNF-a. This result, together with the multimerization behavior of the over-produced TNF-a, was leading us to the assumption that the monomeric form of the protein exhibits the correct tertiary structure.…”