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Molecular Basis of Allosteric Transitions: GroEL

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Macromolecular Crystallography

Abstract

Chaperonins such as GroEL from Escherichia coli are molecular machines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space owing to complex allosteric regulation. Here, we describe some of the various functional (allosteric) states of GroEL, the pathways by which they inter-convert and the coupling between allosteric transitions and protein folding reactions.

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Author information

Authors and Affiliations

  1. Department of Structural Biology, Weizmann Institute of Science, 76100, Rehovot, Israel

    Amnon Horovitz

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  1. Amnon Horovitz
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Correspondence to Amnon Horovitz .

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Editors and Affiliations

  1. , Instit.de Technologia Química e Biológia, Universidade Nova de Lisboa, Rua da Quinta Grande , Apartado 127 6, Oeiras, 2781-901, Portugal

    Maria Armenia Carrondo

  2. Dipto. Scienze Chimiche, Università di Padova, Via F. Marzolo 1, Padova, 35131, Italy

    Paola Spadon

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Horovitz, A. (2012). Molecular Basis of Allosteric Transitions: GroEL. In: Carrondo, M., Spadon, P. (eds) Macromolecular Crystallography. NATO Science for Peace and Security Series A: Chemistry and Biology. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-2530-0_7

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