Protein Aggregation: Opposing Effects of Chaperones and Crowding

  • R. John Ellis


Each molecule of every protein runs the risk that at any time between its synthesis and its degradation, it will bind to one or more identical molecules to form a nonfunctional aggregate. Some protein aggregates are toxic to cells, including neurones, and are thus factors in the development of neurodegenerative and other human diseases. The incidence of such diseases is increasing, together with human longevity and obesity. The probability of protein aggregation is increased by the crowded state of most intracellular compartments, but is reduced by the activities of a diverse range of proteins acting as molecular chaperones. These chaperones use a variety of mechanisms to combat aggregation during the folding of newly synthesized protein chains, their transport into and across membranes, and their assembly into functional oligomers. This article discusses some of the key concepts and basic evidence underlying these conclusions.


Protein Aggregation Molecular Chaperone Amyloid Fibril Trigger Factor Protein Chain 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  1. 1.Department of Biological SciencesUniversity of WarwickCoventryUK

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