title: Structure of a kinetic protein folding intermediate by equilibrium amide exchange.
abstract: A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.
authors.forename: L L
authors.initials: LL
authors.lastname: Hosszu
authors.forename: C J
authors.initials: CJ
authors.lastname: Craven
authors.forename: M J
authors.initials: MJ
authors.lastname: Parker
authors.forename: M
authors.initials: M
authors.lastname: Lorch
authors.forename: J
authors.initials: J
authors.lastname: Spencer
authors.forename: A R
authors.initials: AR
authors.lastname: Clarke
authors.forename: J P
authors.initials: JP
authors.lastname: Waltho
mesh_terms: D000577:Amides; D004795:Enzyme Stability; D001411:Geobacillus stearothermophilus / Q000201:enzymology; D006358:Hot Temperature; D006860:Hydrogen Bonding; D007700:Kinetics; D008958:Models, Molecular; D008962:Models, Theoretical; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000378:metabolism*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D000577:Amides; D010735:Phosphoglycerate Kinase