Effects of positively charged redox molecules on disulfide-coupled protein folding

Masaki Okumura, Shigeru Shimamoto, Takeyoshi Nakanishi, Yu Ichiro Yoshida, Tadafumi Konogami, Shogo Maeda, Yuji Hidaka

Research output: Contribution to journalArticlepeer-review

11 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)3926-3930
Number of pages5
JournalFEBS Letters
Issue number21
Publication statusPublished - 2012 Nov 2


  • Disulfide
  • Folding
  • Glutathione
  • Intermediate
  • Lysozyme
  • Prouroguanylin
  • Thiol


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