Metastability of native proteins and the phenomenon of amyloid formation.

Journal article

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.

Authors: Baldwin, A; Knowles, T; Tartaglia, G; Fitzpatrick, A; Devlin, G

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 133
• Issue: 36
• Pages: 14160-14163
• Publication date: 2011-09-01
• DOI: 10.1021/ja2017703
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Amyloid; Humans; Protein Conformation; Protein Stability; Animals; Entropy; Cattle