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Symmetric complexes of GroE chaperonins as part of the functional cycle.

Schmidt, M. ; Rutkat, K. ; Rachel, Reinhard ; Pfeifer, G. ; Jaenicke, R. ; Viitanen, P. ; Lorimer, G. ; Buchner, J.



Abstract

The particular structural arrangement of chaperonins probably contributes to their ability to assist in the folding of proteins. The interaction of the oligomeric bacterial chaperonin GroEL and its cochaperonin, GroES, in the presence of adenosine diphosphate (ADP) forms an asymmetric complex. However, in the presence of adenosine triphosphate (ATP) or its nonhydrolyzable analogs, symmetric ...

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