Metastability of Native Proteins and the Phenomenon of Amyloid Formation
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- 作者：Andrew J. Baldwin ; Tuomas P. J. Knowles ; Gian Gaetano Tartaglia ; Anthony W. Fitzpatrick ; Glyn L. Devlin ; Sarah Lucy Shammas ; Christopher A. Waudby ; Maria F. Mossuto ; Sarah Meehan ; Sally L. Gras ; John Christodoulou ; Spencer J. Anthony-Cahill ; Paul D. Barker ; Michele Vendruscolo ; Christopher M. Dobson
- 刊名：Journal of the American Chemical Society
- 出版年：2011
- 出版时间：September 14, 2011
- 年：2011
- 卷：133
- 期：36
- 页码：14160-14163
- 全文大小：745K
- 年卷期：v.133,no.36(September 14, 2011)
- ISSN：1520-5126
文摘
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.