Figure 9
From: Prion protein insertional mutations increase aggregation propensity but not fiber stability
The stability of the prion protein fibers is not enhanced by expansion of the repeat domain. (A) Fibers were formed overnight, treated with GdHCl (0 M, 0.5 M, 1.0 M, 1.5 M and 2 M) denaturant and then separated into soluble and pellet fractions by centrifugation (16,000 × g). Samples were analyzed by SDS-PAGE and western blotted using α-Sup35 antibodies. Bands were quantified using ImageJ software. (B) Fibers of SP5NM (●), SP8NM (○), SP11NM (▼) and SP14NM (△) were formed overnight, treated across a temperature gradient in the presence of 2% SDS. Following SDS-PAGE and western blot, gel bands were quantified using ImageJ software and and best fit lines were graphed using SigmaPlot software.