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Abstract
The fluorescence intensity of a unique tryptohan 36 in human interferon-γ was drastically decreased below pH 4 with a concomitant decrease of antiviral activity. The region of residues 32–42 of human interferon-γ was found by calculation to have a low hydrophobicity together with a high helical hydrophobic moment, and the net electric charge of this region having an amphiphilic helical structure changed significantly near pH 4. These results suggest that the region of residues 32–42 plays am important role in exhibiting antiviral activity.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular Enzymology
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