title: Effects of positively charged redox molecules on disulfide-coupled protein folding.
abstract: In vitro folding of disulfide-containing proteins is generally regulated by redox molecules, such as glutathione. However, the role of the cross-disulfide-linked species formed between the redox molecule and the protein as a folding intermediate in the folding mechanism is poorly understood. In the present study, we investigated the effect of the charge on a redox molecule on disulfide-coupled protein folding. Several types of aliphatic thiol compounds including glutathione were examined for the folding of disulfide-containing-proteins, such as lysozyme and prouroguanylin. The results indicate that the positive charge and its dispersion play a critical role in accelerating disulfide-coupled protein folding.
authors.affiliation: Faculty of Science and Engineering, Kinki University, Higashi-Osaka, Osaka, Japan.
authors.forename: Masaki
authors.initials: M
authors.lastname: Okumura
authors.forename: Shigeru
authors.initials: S
authors.lastname: Shimamoto
authors.forename: Takeyoshi
authors.initials: T
authors.lastname: Nakanishi
authors.forename: Yu-ichiro
authors.initials: Y
authors.lastname: Yoshida
authors.forename: Tadafumi
authors.initials: T
authors.lastname: Konogami
authors.forename: Shogo
authors.initials: S
authors.lastname: Maeda
authors.forename: Yuji
authors.initials: Y
authors.lastname: Hidaka
mesh_terms: D056148:Chromatography, Reverse-Phase; D004220:Disulfides / Q000737:chemistry*; D005978:Glutathione / Q000737:chemistry*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009113:Muramidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D017510:Protein Folding; D011498:Protein Precursors / Q000737:chemistry*; D012996:Solutions; D055672:Static Electricity; D013438:Sulfhydryl Compounds / Q000737:chemistry*
chemical_list: D004220:Disulfides; D011498:Protein Precursors; D012996:Solutions; D013438:Sulfhydryl Compounds; C097400:prouroguanylin; D009113:Muramidase; D005978:Glutathione