Details

Autor(en) / Beteiligte

• Baldwin, Andrew J
• Knowles, Tuomas P. J
• Tartaglia, Gian Gaetano
• Fitzpatrick, Anthony W
• Devlin, Glyn L
• Shammas, Sarah Lucy
• Waudby, Christopher A
• Mossuto, Maria F
• Meehan, Sarah
• Gras, Sally L
• Christodoulou, John
• Anthony-Cahill, Spencer J
• Barker, Paul D
• Vendruscolo, Michele
• Dobson, Christopher M

Titel

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

Ist Teil von

• Journal of the American Chemical Society, 2011-09, Vol.133 (36), p.14160-14163

Ort / Verlag

United States: American Chemical Society

Erscheinungsjahr

2011

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.