Modeling of an novel reaction cycle and analyses of cellular dynamics of chaperonin GroEL

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Chaperonin GroEL is involved in the folding of ～15% of newly translated protein in the cell. To clarify the chaperonin reaction mechanism, we analyzed in detail the symmetric football complexes which is critical intermediate in the reaction cycle, and demonstrated asymmetric diversity of two reaction chambers in the football complexes. We also established key techniques for isolating and detecting the chaperonin complexes formed in the cell, and determined the solution structure of the complexes encapsulating its substrate proteins.