Author: Shields, Lauren E.; Jennings, Jordan; Liu, Qinfang; Lee, Jinhwa; Ma, Wenjun; Blecha, Frank; Miller, Laura C.; Sang, Yongming
Title: Cross-Species Genome-Wide Analysis Reveals Molecular and Functional Diversity of the Unconventional Interferon-? Subtype Document date: 2019_6_25
ID: 14gcu1se_55
Snippet: Compared with the classical IFN-α subtype, the antiviral activity of porcine IFN-ω peptides (especially IFN IFN-ω5) showed similar acidic stability but higher resistance to heat treatments ( Table 1) . Increased thermostability is correlated to the increase in the number of hydrogen bonds and in polar surface area fraction of a protein (44) . We interpret that the thermal stability of some IFN-ω peptides may reflect their property in tertiary.....
Document: Compared with the classical IFN-α subtype, the antiviral activity of porcine IFN-ω peptides (especially IFN IFN-ω5) showed similar acidic stability but higher resistance to heat treatments ( Table 1) . Increased thermostability is correlated to the increase in the number of hydrogen bonds and in polar surface area fraction of a protein (44) . We interpret that the thermal stability of some IFN-ω peptides may reflect their property in tertiary structure, which in turn may contribute to the broader and higher antiviral activity by the affinity of the IFN ligand-receptor interaction (29) . Currently, there are few, if any, studies comparing the affinity difference between IFN-ω and IFN-α/β to the common IFN receptors of IFNAR1/2 (29) .
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