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Effects of positively charged redox molecules on disulfide‐coupled protein folding
Author(s) -
Okumura Masaki,
Shimamoto Shigeru,
Nakanishi Takeyoshi,
Yoshida Yu-ichiro,
Konogami Tadafumi,
Maeda Shogo,
Hidaka Yuji
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.09.031
Subject(s) - folding (dsp implementation) , chemistry , protein folding , oxidative folding , redox , protein disulfide isomerase , biophysics , disulfide bond , glutathione , thiol , phi value analysis , molecule , glutathione disulfide , lysozyme , biochemistry , organic chemistry , enzyme , biology , electrical engineering , engineering
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.