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Nature 442, 360-362 (27 July 2006) | doi:10.1038/442360a; Published online 26 July 2006
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Protein folding: Inside the cage
R. John Ellis1
Abstract
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.
Proteins are the action molecules of life, but cells face a problem in making them. Proteins consist of amino acids joined into linear polypeptide chains by intracellular structures called ribosomes.
- R. John Ellis is in the Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK.
Email: jellis@bio.warwick.ac.uk
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