title: Reexamination of the folding of BPTI: predominance of native intermediates.
abstract: Bovine pancreatic trypsin inhibitor (BPTI) continues to be the only protein for which a detailed pathway of folding has been described. Previous studies led to the conclusion that nonnative states are well populated in the oxidative folding of BPTI. This conclusion has broadly influenced efforts to understand protein folding. The population of intermediates present during the folding of BPTI has been reexamined by modern separation techniques. It was found that all well-populated folding intermediates contain only native disulfide bonds. These data emphasize the importance of native protein structure for understanding protein folding.
authors.affiliation: Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Cambridge, MA 02142.
authors.forename: J S
authors.initials: JS
authors.lastname: Weissman
authors.forename: P S
authors.initials: PS
authors.lastname: Kim
mesh_terms: D000595:Amino Acid Sequence; D007611:Aprotinin / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D004220:Disulfides / Q000032:analysis; D007202:Indicators and Reagents; D008961:Models, Structural; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D011487:Protein Conformation
chemical_list: D004220:Disulfides; D007202:Indicators and Reagents; D010446:Peptide Fragments; D007611:Aprotinin