The circular dichroism of tumor necrosis factor‐α: Measurement into the vacuum UV and analysis for secondary structure

Abstract

The circular dichroism (CD) spectrum of tumor necrosis factor-alpha has been measured into the vacuum UV to 168 nm. Analysis of the CD for secondary structure is in good agreement with X-ray diffraction results, but the analysis is somewhat unstable. Adding the CD of this protein together with its X-ray determined secondary structure to the basis set should improve subsequent analyses of CD spectra for other all-beta proteins.

Recombinant production of bioactive human TNF-α by SUMO-fusion system – High yields from shake-flask culture

“…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.…”