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Chaperonins are molecular machines that undergo large-scale ATP-driven conformational changes that are crucial for their protein folding function. These changes are concerted in the case of the prokaryotic chaperonin GroEL and sequential in the case of the eukaryotic chaperonin CCT. Experiments (1, 2) and lattice model simulations (3) that explore the implications of these different allosteric mechanisms for the folding function of chaperonins will be described.
References 1. Kipnis, Y., Papo, N., Haran, G. & Horovitz, A. (2007) Proc. Natl. Acad. Sci. USA 104, 3119-3124. 2. Papo, N., Kipnis, Y., Haran, G. & Horovitz, A. (2008) J. Mol. Biol. 380, 717-725. 3. Jacob, E., Horovitz, A. & Unger, R. (2007) Bioinformatics 23, i240-i248. |
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