Conformations of fibroblast and E. coli-derived recombinant human interferon-beta s as studied by nuclear magnetic resonance and circular dichroism.
The conformations of fibroblast and E. coli-derived recombinant human interferon-beta s 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 alpha-helix contents (approximately 70%). These results suggest that glycosylation does not appreciably change the conformation of human interferon-beta. Moreover, a slow conformational change is observed below pH 2.0, which induces the disruption of beta-sheets.
D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007370:Interferon Type I / Q000096:biosynthesis; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011522:Protons; D011994:Recombinant Proteins / Q000096:biosynthesis
D007370:Interferon Type I; D011522:Protons; D011994:Recombinant Proteins