title: Metastability of native proteins and the phenomenon of amyloid formation.
abstract: An experimental determination of the thermodynamic stabilities of a series of amyloid fibrils reveals that this structural form is likely to be the most stable one that protein molecules can adopt even under physiological conditions. This result challenges the conventional assumption that functional forms of proteins correspond to the global minima in their free energy surfaces and suggests that living systems are conformationally as well as chemically metastable.
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
authors.forename: Andrew J
authors.initials: AJ
authors.lastname: Baldwin
authors.forename: Tuomas P J
authors.initials: TP
authors.lastname: Knowles
authors.forename: Gian Gaetano
authors.initials: GG
authors.lastname: Tartaglia
authors.forename: Anthony W
authors.initials: AW
authors.lastname: Fitzpatrick
authors.forename: Glyn L
authors.initials: GL
authors.lastname: Devlin
authors.forename: Sarah Lucy
authors.initials: SL
authors.lastname: Shammas
authors.forename: Christopher A
authors.initials: CA
authors.lastname: Waudby
authors.forename: Maria F
authors.initials: MF
authors.lastname: Mossuto
authors.forename: Sarah
authors.initials: S
authors.lastname: Meehan
authors.forename: Sally L
authors.initials: SL
authors.lastname: Gras
authors.forename: John
authors.initials: J
authors.lastname: Christodoulou
authors.forename: Spencer J
authors.initials: SJ
authors.lastname: Anthony-Cahill
authors.forename: Paul D
authors.initials: PD
authors.lastname: Barker
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
mesh_terms: D000682:Amyloid / Q000737:chemistry*; D000818:Animals; D002417:Cattle; D019277:Entropy; D006801:Humans; D011487:Protein Conformation; D055550:Protein Stability
chemical_list: D000682:Amyloid