Conformations of Fibroblast and E. coli-Derived Recombinant Human Interferon-βs as Studied by Nuclear Magnetic Resonance and Circular Dichroism

Abstract

The conformations of fibroblast and E. coli-derived recombinant human interferon-βs were studied by circular dichroism and nuclear magnetic resonance spectroscopy in the acidic pH region of 4.6 to 1.6. Both interferons have very similar conformations with high α-helix contents (_??_70%). These results suggest that glycosylation does not appreciably change the conformation of human interferon-β. Moreover, a slow conformational change is observed below pH 2.0, which induces the disruption of β-sheets.