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“Native‐like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications
Author(s) -
Bemporad Francesco,
Chiti Fabrizio
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.013
Subject(s) - sulfolobus solfataricus , circumstantial evidence , amyloid (mycology) , chemistry , sulfolobus , native state , protein aggregation , biophysics , biology , biochemistry , archaea , geography , inorganic chemistry , archaeology , gene
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.