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. © 2011 American Chemical Society.

Metastability of native proteins and the phenomenon of amyloid formation / Baldwin, A. J.; Knowles, T. P. J.; Tartaglia, G. G.; Fitzpatrick, A. W.; Devlin, G. L.; Shammas, S. L.; Waudby, C. A.; Mossuto, M. F.; Meehan, S.; Gras, S. L.; Christodoulou, J.; Anthony-Cahill, S. J.; Barker, P. D.; Vendruscolo, M.; Dobson, C. M.. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - 133:36(2011), pp. 14160-14163. [10.1021/ja2017703]

Metastability of native proteins and the phenomenon of amyloid formation

Tartaglia G. G.;Vendruscolo M.;
2011

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. © 2011 American Chemical Society.
2011
Amyloid; Animals; Cattle; Entropy; Humans; Protein Conformation; Protein Stability
01 Pubblicazione su rivista::01a Articolo in rivista
Metastability of native proteins and the phenomenon of amyloid formation / Baldwin, A. J.; Knowles, T. P. J.; Tartaglia, G. G.; Fitzpatrick, A. W.; Devlin, G. L.; Shammas, S. L.; Waudby, C. A.; Mossuto, M. F.; Meehan, S.; Gras, S. L.; Christodoulou, J.; Anthony-Cahill, S. J.; Barker, P. D.; Vendruscolo, M.; Dobson, C. M.. - In: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY. - ISSN 0002-7863. - 133:36(2011), pp. 14160-14163. [10.1021/ja2017703]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1451766
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