title: Protein aggregation starting from the native globular state.
abstract: Amyloid formation by globular proteins that normally adopt a compact folded structure is generally induced in vitro under harsh conditions involving low pH, high temperature, high pressure, or in the presence of organic solvents. Under these conditions, folded proteins are generally unfolded, at least partially. The approach described here shows a rationale and two detailed examples as to how the mechanism of aggregation of a globular protein can be probed under conditions in which it is initially in its folded conformation, and hence relevant to a physiological environment.
authors.affiliation: Università di Firenze, Dipartimento di Scienze Biochimiche, Firenze, Italy.
authors.forename: Giordana
authors.initials: G
authors.lastname: Marcon
authors.forename: Georgia
authors.initials: G
authors.lastname: Plakoutsi
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Chiti
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D019878:Carboxyl and Carbamoyl Transferases; D029968:Escherichia coli Proteins; D006801:Humans; D007700:Kinetics; D011487:Protein Conformation; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D011506:Proteins / Q000737:chemistry*; D048229:Sulfolobus solfataricus / Q000201:enzymology; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D001426:Bacterial Proteins; D019878:Carboxyl and Carbamoyl Transferases; D029968:Escherichia coli Proteins; D011506:Proteins; D000097024:Acylphosphatase; C108878:HypF protein, Bacteria; C504838:hypF protein, E coli