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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


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Protein aggregation in crowded environments

R. John Ellis1 / Allen P. Minton2

1.

2.

Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 5, Pages 485–497, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.064, June 2006

Publication History

Published Online:
2006-06-01

Abstract

The generic tendency of proteins to aggregate into non-functional, and sometimes cytotoxic, structures poses a universal problem for all types of cell. This tendency is greatly exacerbated by the high total concentration of macromolecules found within most intracellular compartments, a phenomenon referred to as macromolecular crowding. This review discusses the quantitative effects of crowding on protein aggregation and the role of molecular chaperones in combating this problem.

Keywords: excluded volume; macromolecular crowding; molecular chaperones; protein aggregation; protein folding

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