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.| File | Dimensione | Formato | |
|---|---|---|---|
|
Baldwin_Metastability_2020.pdf
accesso aperto
Tipologia:
Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza:
Tutti i diritti riservati (All rights reserved)
Dimensione
1.05 MB
Formato
Adobe PDF
|
1.05 MB | Adobe PDF |
I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
