Protein aggregation in crowded environments

Biol Chem. 2006 May;387(5):485-97. doi: 10.1515/BC.2006.064.

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.

Publication types

  • Review

MeSH terms

  • Algorithms
  • Animals
  • Humans
  • Macromolecular Substances / chemistry*
  • Macromolecular Substances / metabolism
  • Models, Biological
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Protein Binding
  • Protein Denaturation
  • Protein Folding
  • Proteins / chemistry*
  • Proteins / metabolism

Substances

  • Macromolecular Substances
  • Molecular Chaperones
  • Proteins