Abstract
The vast majority of theoretical and experimental folding studies have shown that as a protein folds, it attempts to adopt a conformation that occurs at its lowest free energy minimum. However, studies on a small number of proteins have now shown that this is a generality. In this review we discuss recent data on how two proteins, α-lytic protease and α1-antitrypsin, successfully fold to their metastable native states, whilst avoiding more stable but inactive conformations.
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Acknowledgements
SPB would like to thank members of his laboratory for their time and effort. SPB is a Monash University Senior Logan Research Fellow and an RD Wright Fellow of the NH&MRC. This work is supported by the NH&MRC and the Australian Research Council.
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Cabrita, L.D., Bottomley, S.P. How do proteins avoid becoming too stable? Biophysical studies into metastable proteins. Eur Biophys J 33, 83–88 (2004). https://doi.org/10.1007/s00249-003-0356-1
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DOI: https://doi.org/10.1007/s00249-003-0356-1