Protein aggregation in crowded environments.
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.
Ellis
R John
RJ
Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK. jellis@bio.warwick.ac.uk
Minton
Allen P
AP
D000465:Algorithms; D000818:Animals; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry* / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism
D046911:Macromolecular Substances; D018832:Molecular Chaperones; D011506:Proteins