Effects of macromolecular crowding on protein folding and aggregation
UNSPECIFIED. (1999) Effects of macromolecular crowding on protein folding and aggregation. EMBO JOURNAL, 18 (24). pp. 6927-6933. ISSN 0261-4189Full text not available from this repository.
We have studied the effects of polysaccharide and protein crowding agents on the refolding of oxidized and reduced hen lysozyme in order to test the prediction that association constants of interacting macromolecules in living cells are greatly increased by macromolecular crowding relative to their values in dilute solutions. We demonstrate that whereas refolding of oxidized lysozyme is hardly affected by crowding, correct refolding of the reduced protein is essentially abolished due to aggregation at high concentrations of crowding agents. The results show that the protein folding catalyst protein disulfide isomerase is particularly effective in preventing lysozyme aggregation under crowded conditions, suggesting that crowding enhances its chaperone activity. Our findings suggest that the effects of macromolecular crowding could have major implications for our understanding of how protein folding occurs inside cells.
|Item Type:||Journal Article|
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Journal or Publication Title:||EMBO JOURNAL|
|Publisher:||OXFORD UNIV PRESS|
|Date:||15 December 1999|
|Number of Pages:||7|
|Page Range:||pp. 6927-6933|
Actions (login required)