ArticleJournal of the American Society for Mass Spectrometry2012
A negative ion mass spectrometry approach to identify cross-linked peptides utilizing characteristic disulfide fragmentations.
Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 17 citations in OpenAlex.
- Probing Protein 3D Structures and Conformational Changes Using Electrochemistry-Assisted Isotope Labeling Cross-Linking Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016Article
- Integration of electrochemistry with ultra-performance liquid chromatography/mass spectrometry.European journal of mass spectrometry (Chichester, England) · 2015Article
- Cross-linking electrochemical mass spectrometry for probing protein three-dimensional structures.Analytical chemistry · 2014Article
- Integration of online digestion and electrolytic reduction with mass spectrometry for rapid disulfide-containing protein structural analysis.International journal of mass spectrometry · 2013Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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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.
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