Figure 4 | Scientific Reports

Figure 4

From: Complex folding and misfolding effects of deer-specific amino acid substitutions in the β2-α2 loop of murine prion protein

Figure 4

Oligomerisation of the murine PrP variants.

Panels (A–D) represent typical size exclusion chromatograms over a time course of oligomerisation of (A) recMoPrP; (B) recMoPrP-S169N; (C) recMoPrP-N173T; (D) recMoPrP-S169N/N173T. Samples were incubated at 45 °C in oligomerisation buffer and aliquots were removed from the reaction every 15 minutes from 0 (lightest trace) to 105 minutes (darkest trace) for analysis. Oligomerisation was performed at least 4 times for each variant, the area under each peak was calculated and plotted as a function of time for (E) recMoPrP; (F) recMoPrP-S169N; (G) recMoPrP-N173T; (H) recMoPrP-S169N/N173T. •–peak 1 (large oligomer) ■–peak 2 (small oligomer) ▲–peak 3 (monomeric protein). Error bars represent the standard deviations.

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