Thermodynamic measurements show that the most stable structural form of a number of proteins under cellular conditions is fibrillar, implying that their functional states may only be metastable.
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References
Baldwin, A. J. et al. J. Am. Chem. Soc. 133, 14160–14163 (2011).
Kodali, R. & Wetzel, R. Curr. Opin. Struct. Biol. 17, 48–57 (2007).
Oosawa, F. & Kasai, M. J. Mol. Biol. 4, 10–21 (1962).
Honeycutt, J. D. & Thirumalai, D. Proc. Natl Acad. Sci. 87, 3526–3529 (1990).
Dinner, A. R. & Karplus, M. Nature Struct. Biol. 5, 236–241 (1998).
Thirumalai, D., Klimov, D. K. & Dima, R. I. Curr. Opin. Struct. Biol. 13, 146–159 (2003).
Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Science 319, 916–919 (2008).
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Thirumalai, D., Reddy, G. Are native proteins metastable?. Nature Chem 3, 910–911 (2011). https://doi.org/10.1038/nchem.1207
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DOI: https://doi.org/10.1038/nchem.1207
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