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Metastability of Native Proteins and the Phenomenon of Amyloid Formation

Baldwin, AJ; Knowles, TPJ; Tartaglia, GG; Fitzpatrick, AW; Devlin, GL; Shammas, SL; Waudby, CA; ... Dobson, CM; + view all (2011) Metastability of Native Proteins and the Phenomenon of Amyloid Formation. J AM CHEM SOC , 133 (36) 14160 - 14163. 10.1021/ja2017703.

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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.

Type: Article
Title: Metastability of Native Proteins and the Phenomenon of Amyloid Formation
DOI: 10.1021/ja2017703
Keywords: FIBRILS, STABILITY, PEPTIDE, DISEASE
UCL classification: UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/1311505
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