Fig. 1: Cell-free synthesis of amyloid proteins, illustrated with the prion-forming domain of HET-s. | Communications Biology

Fig. 1: Cell-free synthesis of amyloid proteins, illustrated with the prion-forming domain of HET-s.

From: Cell-free synthesis of amyloid fibrils with infectious properties and amenable to sub-milligram magic-angle spinning NMR analysis

Fig. 1

a Schematic representation of the production of cell-free synthesized HET-s amyloid fibrils. RM: reaction mixture. FM: Feeding mixture. b RM is harvested using centrifugation and washed to obtain the NMR sample. c Electron micrograph of CF synthesized HET-s PFD amyloid fibrils. Scale bar: 100 nm. d CF-synthesized HET-s PFD triggers the phenotypic conversion of [Het-s*] strains (infection) detected as a regulated cell death reaction as observed by the barrage reaction (yellow arrow) when the focal strain in the center of the plate is confronted to the four [Het-S] strains at the periphery.

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