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Fig. 1 | BMC Biology

Fig. 1

From: Protein assembly systems in natural and synthetic biology

Fig. 1

Overview of higher-order assemblies. a Protein assemblies display a spectrum of material properties, from solid-like amyloid fibers to highly dynamic liquid droplets. Examples of assemblies are shown below the spectrum. Highly stable assemblies include MAVS (mitochondrial antiviral signaling) protein fibers and Aβ (amyloid β) peptide amyloid fibrils. Highly dynamic assemblies include nucleoli, membraneless organelles with liquid-like shell around a more organized rigid core. The yeast prion protein Sup35 can convert between different structures: it constructs stable amyloid fibrils in its prion conformation and undergoes reversible gel formation under pH stress. Stress granules and P-bodies can also exist in different states, depending on the physiology of the cell. b Prions are self-propagating protein conformations. The prion conformation (purple) serves as a template to convert the soluble (gray) conformation into the prion conformation, which usually results in the growth of amyloid aggregates. The aggregates are fragmented by chaperone proteins, producing seeds that can nucleate the conformational conversion

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