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Deducing disulfide patterns of cysteine-rich proteins using signature fragments produced by top-down mass spectrometry

Abstract

Direct mapping of protein disulfide pattern using top-down mass spectrometry (MS) is often hampered by inadequate fragmentation at the disulfide-enclosing region, and insufficient structural information provided by the fragments. Here we used electron-transfer/high energy collision dissociation (EThcD) to improve the fragmentation efficiency, and developed strategies that minimize false positive identification of fragments and deconvolute signals representing specific modifications made to the disulfide-cleavage-induced fragments. We observed clear correlations between unique modification (attachment or removal of H or SH) pattern and the number of disulfide bonds that enclose the corresponding region. Using the characteristic signature fragments, we in part localized Cys-bridging sites in disulfide-scrambled lysozyme, and reduced the number of putative disulfide patterns from 104 to 6. The results demonstrated the feasibility of direct analysis of complex disulfide patterns using top-down MS.

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Supplementary files

Publication details

The article was received on 01 Oct 2017, accepted on 02 Jan 2018 and first published on 04 Jan 2018


Article type: Communication
DOI: 10.1039/C7AN01625E
Citation: Analyst, 2018, Accepted Manuscript
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    Deducing disulfide patterns of cysteine-rich proteins using signature fragments produced by top-down mass spectrometry

    X. Zhao, Y. Shen, W. Tong, G. Wang and D. D. Y. Chen, Analyst, 2018, Accepted Manuscript , DOI: 10.1039/C7AN01625E

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