title: Dynamic prions revealed by magic.
abstract: Prion proteins can be propagated as amyloid fibrils with several different conformational variants. By providing structural information at atomic level for two such variants of a yeast prion, Frederick and colleagues, in this issue of Chemistry & Biology, reveal how conformational flexibility can generate phenotypic diversity.
authors.affiliation: Kent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK. Electronic address: m.f.tuite@kent.ac.uk.
authors.forename: Mick F
authors.initials: MF
authors.lastname: Tuite
authors.affiliation: Protein Science Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Howard
authors.affiliation: Kent Fungal Group, School of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.
authors.forename: Wei-Feng
authors.initials: WF
authors.lastname: Xue
mesh_terms: D000682:Amyloid / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D011328:Prions / Q000378:metabolism*
chemical_list: D000682:Amyloid; D018832:Molecular Chaperones; D011328:Prions