| Literature DB >> 21650202 |
Andrew J Baldwin1, 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.
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.Entities:
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Year: 2011 PMID： 21650202 DOI： 10.1021/ja2017703
Source DB: PubMed Journal: J Am Chem Soc ISSN： 0002-7863 Impact factor: 15.419