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Identification of intramolecular disulfide bonds in GrxS12

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NIAID Data Ecosystem2026-05-10 收录
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https://www.omicsdi.org/dataset/pride/PXD058877
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To investigate whether the conserved Cys residues of Grxs form intramolecular or intermolecular disulfide bonds, the recombinant GrxS12 proteins were purified, and subsequently separated using non-reducing SDS-PAGE. The gel revealed the presence of a monomer band but not a dimer band, indicating the absence of intermolecular disulfide bonds. The protein from the monomer band was subjected to proteolytic digestion and subsequent analysis by spectrometry. The spectrometric data revealed that the GrxS12 formed an intramolecular disulfide linkage between the T31WJC34SYSSQVK41 and H88IGGC92SDTLQLHNKGELEAILAEANGK114 peptides.
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2026-01-16
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