Author: MJ Morwitzer; A Corona; L Zinzula; E Fanunza; C Nigri; S Distinto; C Vornholt; V Kumar; E Tramontano; SP Reid
Title: Mutation of Ebola virus VP35 Ser129 uncouples interferon antagonist and replication functions Document date: 2019_8_7
ID: cbyzdnrp_63
Snippet: ( Figure 2E ). Consistent with this hypothesis, deconvolution of CD spectra and analysis of the 425 secondary structure content showed that the VP35 S129A oligomerization domain has a lower 426 -helical percentage with respect to WT at all temperature values tested, and that this content 427 diminishes as temperature increases ( Figure 2F ). This result indicates that a more flexible and 428 relaxed conformation is applied at the level of the VP3.....
Document: ( Figure 2E ). Consistent with this hypothesis, deconvolution of CD spectra and analysis of the 425 secondary structure content showed that the VP35 S129A oligomerization domain has a lower 426 -helical percentage with respect to WT at all temperature values tested, and that this content 427 diminishes as temperature increases ( Figure 2F ). This result indicates that a more flexible and 428 relaxed conformation is applied at the level of the VP35 coiled-coil superhelix upon the 429 substitution of Ser-to-Ala at residue 129. 430
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