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https://hdl.handle.net/2440/74819
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Type: | Journal article |
Title: | A negative ion mass spectrometry approach to identify cross-linked peptides utilizing characteristic disulfide fragmentations |
Author: | Calabrese, A. Good, N. Wang, T. He, J. Bowie, J. Pukala, T. |
Citation: | Journal of the American Society for Mass Spectrometry, 2012; 23(8):1364-1375 |
Publisher: | Elsevier Science |
Issue Date: | 2012 |
ISSN: | 1044-0305 1879-1123 |
Statement of Responsibility: | Antonio N. Calabrese, Nikki J. Good, Tianfang Wang, Jingjia He, John H. Bowie, Tara L. Pukala |
Abstract: | Chemical cross-linking combined with mass spectrometry (MS) is an analytical tool used to elucidate the topologies of proteins and protein complexes. However, identification of the low abundance cross-linked peptides and modification sites amongst a large quantity of proteolytic fragments remains challenging. In this work, we present a strategy to identify cross-linked peptides by negative ion MS for the first time. This approach is based around the facile cleavages of disulfide bonds in the negative mode, and allows identification of cross-linked products based on their characteristic fragmentations. MS(3) analysis of the cross-linked peptides allows for their sequencing and identification, with residue specific location of cross-linking sites. We demonstrate the applicability of the commercially available cystine based cross-linking reagent dithiobis(succinimidyl) propionate (DSP) and identify cross-linked peptides from ubiquitin. In each instance, the characteristic fragmentation behavior of the cross-linked species is described. The data presented here indicate that this negative ion approach may be a useful tool to characterize the structures of proteins and protein complexes, and provides the basis for the development of high throughput negative ion MS chemical cross-linking strategies. |
Keywords: | Negative ion mass spectrometry Chemical cross-linking Disulfide fragmentations Protein structure determination |
Rights: | © Springer, Part of Springer Science+Business Media |
DOI: | 10.1007/s13361-012-0407-x |
Grant ID: | http://purl.org/au-research/grants/arc/DP1093143 |
Published version: | http://dx.doi.org/10.1007/s13361-012-0407-x |
Appears in Collections: | Aurora harvest 4 IPAS publications |
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