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Protein thermodynamics

Are native proteins metastable?

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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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Figure 1: Schematic energy landscape for folding and aggregation.

References

  1. Baldwin, A. J. et al. J. Am. Chem. Soc. 133, 14160–14163 (2011).

    Article  CAS  Google Scholar 

  2. Kodali, R. & Wetzel, R. Curr. Opin. Struct. Biol. 17, 48–57 (2007).

    Article  CAS  Google Scholar 

  3. Oosawa, F. & Kasai, M. J. Mol. Biol. 4, 10–21 (1962).

    Article  CAS  Google Scholar 

  4. Honeycutt, J. D. & Thirumalai, D. Proc. Natl Acad. Sci. 87, 3526–3529 (1990).

    Article  CAS  Google Scholar 

  5. Dinner, A. R. & Karplus, M. Nature Struct. Biol. 5, 236–241 (1998).

    Article  CAS  Google Scholar 

  6. Thirumalai, D., Klimov, D. K. & Dima, R. I. Curr. Opin. Struct. Biol. 13, 146–159 (2003).

    Article  CAS  Google Scholar 

  7. Balch, W. E., Morimoto, R. I., Dillin, A. & Kelly, J. W. Science 319, 916–919 (2008).

    Article  CAS  Google Scholar 

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Correspondence to D. Thirumalai.

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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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