@article {C7AN01625E,
	title = {Deducing disulfide patterns of cysteine-rich proteins using signature fragments produced by top-down mass spectrometry},
	journal = {Analyst},
	volume = {143},
	year = {2018},
	month = {01/2018},
	pages = {817-823},
	publisher = {The Royal Society of Chemistry},
	chapter = {817},
	abstract = {<p>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.</p>},
	doi = {10.1039/C7AN01625E},
	url = {http://dx.doi.org/10.1039/C7AN01625E},
	author = {Zhao, Xiuxiu and Shen, Yue and Tong, Wenjun and Wang, Guanbo and Chen, David Da Yong}
}
