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- Title
“Native-like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications
- Authors
Bemporad, Francesco; Chiti, Fabrizio
- Abstract
Abstract: Studies in vitro show that globular proteins can experience the formation of native-like conformational states able to self-assemble with no need of transitions across the energy barrier for unfolding, and that such processes can lead eventually to the formation of amyloid-like species. Circumstantial evidence collected in vivo suggests that aggregation of native-like states can be a concrete possibility for living organisms and thus more relevant than previously thought. In this review we summarize the key observations collected on the “native-like aggregation” of the acylphosphatase from Sulfolobus solfataricus, a protein that has allowed the direct monitoring and analysis of native-like aggregates for its propensity to form rapidly native-like aggregates and their slow conversion into amyloid-like aggregates.
- Subjects
CELL aggregation; GLOBULAR proteins; ENZYMES; MOLECULAR self-assembly; PROTEIN folding; AMYLOID; DROSOPHILA melanogaster; BACTERIAL genomes
- Publication
FEBS Letters, 2009, Vol 583, Issue 16, p2630
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2009.07.013