Related references
Note: Only part of the references are listed.Perturbed ATPase activity and not close confinement of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
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BeFx stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers
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Substrate polypeptide presents a load on the apical domains of the chaperonin GroEL
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Directed evolution of substrate-optimized GroEL/S chaperonins
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Protein folding - Molecular chaperones in the cytosol: from nascent chain to folded protein
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GroEL/GroES-mediated folding of a protein too large to be encapsulated
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Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP
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BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY (2001)