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AAS distributions for static and dynamic protein conformations.
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posted on 2023-01-24, 18:35 authored by Sören von Bülow, Mateusz Sikora, Florian E. C. Blanc, Roberto Covino, Gerhard HummerCumulative distribution functions (CDFs) of static protein structure without glycosylation (A), with GlycoSHIELD glycosylation (B), and CDFs of fully dynamic simulated protein structure without glycosylation (C) and with glycosylation (D). CDFs of the scores are shown for all residues (black); surface residues (blue); mutation sites at the surface of Omicron BA.1 (green), Omicron BA.5 (purple), and earlier variants (orange). The KS statistic is the maximum vertical gap between the respective CDFs, as indicated by red arrows.
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host immune defensebased immune responsessteric shielding effectnewly emerging sarsexpected mutation activityantibody accessibility scoreaas correlate stronglyvariant spike proteinsomicron variant bahigh calculated escapabilityspike surface mutationssteric accessibilitymutation activityspike proteinsincluding omicronhigh valuesescape antibodyspike proteinxlink ">viral evolutiontime viewstrong predictorsteady emergenceprior infectionprimary targetpinpoint regionsearlier variantse .,available early1 infection