Many newly synthesized bacterial proteins avoid aggregation by folding inside a chaperonin nanocage. Unexpectedly, it turns out that the cage's internal properties can be optimized to accelerate folding.
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References
Ellis, R. J. in Molecular Chaperones and Cell Signalling (eds Henderson, B. & Pockley, G.) 3–21 (Cambridge Univ. Press, 2005).
Saibil, H. R. & Ranson, N. A. Trends Biochem. Sci. 27, 627–632 (2002).
Fenton, W. A. & Horwich, A. L. Q. Rev. Biophys. 36, 229–256 (2003).
Brinker, A. et al. Cell 107, 223–233 (2001).
Tang, Y. -C. et al. Cell 125, 903–914 (2006).
Ellis, R. J. Fold. Des. 1, R9–R15 (1996).
Kerner, M. J. et al. Cell 122, 209–220 (2005).
Minton, A. P. J. Biol. Chem. 276, 10577–10580 (2001).
Ellis, R. J. & Minton, A. P. Biol. Chem. 387, 485–497 (2006).
Xu, Z. H. et al. Nature 388, 741–749 (1997).
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Ellis, R. Inside the cage. Nature 442, 360–361 (2006). https://doi.org/10.1038/442360a
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DOI: https://doi.org/10.1038/442360a
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