作者
Andrew J Baldwin, Tuomas PJ 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
发表日期
2011/9/14
期刊
Journal of the American Chemical Society
卷号
133
期号
36
页码范围
14160-14163
出版商
American Chemical Society
简介
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.
学术搜索中的文章
AJ Baldwin, TPJ Knowles, GG Tartaglia, AW Fitzpatrick… - Journal of the American Chemical Society, 2011