title: Mechanism of protein folding. IV. Forming and breaking of disulfide bonds in bovine pancreatic tripsin inhibitor.
abstract: The folding mechanism of bovine pancreatic tripsin inhibitor (BPTI) is explained theoretically on the basis of the island model, where the driving force of folding is hydrophobic interaction. For this purpose, we take a look at the formation and breaking of disulfide bonds during the folding process of BPTI. The intermediate conformations and the native one are successfully obtained, which satisfy the so-called "lampshade" geometrical criterion for the formation of the disulfide bonds. The folding pathway is consistent with the renaturation experiment by Creighton. In addition, an elaborate treatment of side chains of amino acid residues by the software programme CHARMm confirms quantitatively the formation of disulfide bridges.
authors.affiliation: Frontier Research Program, RIKEN Institute, Saitama, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Kobayashi
authors.forename: H
authors.initials: H
authors.lastname: Sasabe
authors.forename: T
authors.initials: T
authors.lastname: Akutsu
authors.forename: N
authors.initials: N
authors.lastname: Saitô
mesh_terms: D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002417:Cattle; D004220:Disulfides; D008433:Mathematics; D008958:Models, Molecular; D011487:Protein Conformation; D017510:Protein Folding
chemical_list: D004220:Disulfides; D007611:Aprotinin