| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10871267 | FEBS Letters | 2012 | 5 Pages |
Abstract
⺠Roles of cross-disulfide molecules in disulfide-coupled protein folding are proposed. ⺠Several types of aliphatic thiol compounds were examined for protein folding. ⺠Effects of the charge and molecular size of redox molecules were investigated. ⺠A larger ASA+ of thiol reagents is preferred for disulfide-coupled protein folding.
Keywords
MPAGSH and GSSGrCGAETRP-HPLCTFA2-AminoethanethiolTrifluoroacetic acidMercaptopropionic acidFoldingTris(hydroxymethyl)aminomethane hydrochlorideThiolintermediateDisulfideMatrix-assisted Laser Desorption Ionization Time of Flight mass spectrometrylysozymemercaptoethanolMALDI-TOF/MSreversed-phase high performance liquid chromatographyGlutathione
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Authors
Masaki Okumura, Shigeru Shimamoto, Takeyoshi Nakanishi, Yu-ichiro Yoshida, Tadafumi Konogami, Shogo Maeda, Yuji Hidaka,