title: Mapping the transition state and pathway of protein folding by protein engineering.
abstract: In the transition state for unfolding of barnase, the hydrophobic core between the major alpha-helix and beta-sheet is somewhat weakened, the C terminus of the major helix is largely intact but its N terminus is exposed and a major loop has been invaded by solvent.
authors.affiliation: MRC Unit for Protein Function and Design, 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: A R
authors.initials: AR
authors.lastname: Fersht
mesh_terms: D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology; D001426:Bacterial Proteins; D007700:Kinetics; D009154:Mutation; D010449:Peptide Mapping / Q000379:methods; D011487:Protein Conformation; D011489:Protein Denaturation; D015202:Protein Engineering / Q000379:methods; D012260:Ribonucleases / Q000235:genetics / Q000302:isolation & purification*; D013816:Thermodynamics
chemical_list: D001426:Bacterial Proteins; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease