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Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks pp 1–13Cite as

Protein Misassembly

Macromolecular Crowding and Molecular Chaperones

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 594))

Abstract

The generic tendency of proteins to misassemble into nonfunctional, and sometimes cytotoxic, structures poses a universal problem for all types of cell. This problem is exacerbated by the high total concentration of macromolecules found within most in-tracellular compartments but it is solved by the actions of molecular chaperones. This review discusses some of the basic evidence and key concepts relating to this conclusion.

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Author information

Authors and Affiliations

  1. Department of Biological Sciences, University of Warwick, Coventry, CV4 7AL, UK

    R. John Ellis

Authors
  1. R. John Ellis
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Editor information

Editors and Affiliations

  1. Department of Medical Chemistry, Semmelweis University, Budapest, Hungary

    Peter Csermely

  2. Institute of Biochemistry, Biological Research Center of the Hungarian Academy of Sciences, Szeged, Hungary

    László Vígh

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© 2007 Landes Bioscience and Springer Science+Business Media

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Ellis, R.J. (2007). Protein Misassembly. In: Csermely, P., Vígh, L. (eds) Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology, vol 594. Springer, New York, NY. https://doi.org/10.1007/978-0-387-39975-1_1

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