title: Transient folding intermediates characterized by protein engineering.
abstract: Kinetic experiments on engineered mutants of barnase detect an intermediate on the folding pathway and allow the mapping of the tertiary interactions of the side chains and their energetics. Many of the interactions present in the final folded state tend to be either fully formed or not formed at all in the intermediate or subsequent transition state for folding, but the hydrophobic core becomes progressively consolidated. These methods in combination with NMR provide extensive structural characterization of the folding intermediate and the sequence of events in the folding pathway.
authors.affiliation: Department of Chemistry, University of Cambridge, UK.
authors.forename: A
authors.initials: A
authors.lastname: Matouschek
authors.forename: J T
authors.initials: JT
authors.lastname: Kellis
authors.forename: L
authors.initials: L
authors.lastname: Serrano
authors.forename: M
authors.initials: M
authors.lastname: Bycroft
authors.forename: A R
authors.initials: AR
authors.lastname: Fersht
mesh_terms: D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009154:Mutation; D011487:Protein Conformation; D015202:Protein Engineering; D012260:Ribonucleases / Q000235:genetics; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease