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. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Okumura, M., Shimamoto, S., Nakanishi, T., Yoshida, Y. I., Konogami, T., Maeda, S., & Hidaka, Y. (2012). Effects of positively charged redox molecules on disulfide-coupled protein folding. FEBS Letters, 586(21), 3926–3930. https://doi.org/10.1016/j.febslet.2012.09.031