ArticleJournal of the American Society for Mass Spectrometry2012
A pseudo MS3 approach for identification of disulfide-bonded proteins: uncommon product ions and database search.
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 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Mobility-Assisted Pseudo-MSJournal of the American Society for Mass Spectrometry · 2024Article
- A spectroscopic test suggests that fragment ion structure annotations in MS/MS libraries are frequently incorrect.Communications chemistry · 2024Article
- Characterizing the top-down sequencing of protein ions prior to mobility separation in a timsTOF.The Analyst · 2023Article
- Transthyretin proteoforms of intraocular origin in human subretinal fluid.Experimental eye research · 2022Article
- Profiling of Chlorogenic Acids fromMetabolites · 2020Article
- Top-down mass spectrometry of intact phosphorylated β-casein: Correlation between the precursor charge state and internal fragments.Journal of mass spectrometry : JMS · 2019Article
- Revisiting Fragmentation Reactions of Protonated α-Amino Acids by High-Resolution Electrospray Ionization Tandem Mass Spectrometry with Collision-Induced Dissociation.Scientific reports · 2019Article
- Top-Down Protein Identification using a Time-of-Flight Mass Spectrometer and Data Independent Acquisition.International journal of mass spectrometry · 2019Article
- Article
- Review
- Identification of process related trace level impurities in the actinide decorporation agent 3,4,3-LI(1,2-HOPO): Nozzle-skimmer fragmentation via ESI LC-QTOFMS.Journal of pharmaceutical and biomedical analysis · 2014Article
- Fragmentation follows structure: top-down mass spectrometry elucidates the topology of engineered cystine-knot miniproteins.PloS one · 2014Article
- Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1.PloS one · 2013Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has previously been reported that disulfide and backbone bonds of native intact proteins can be concurrently cleaved using electrospray ionization (ESI) and collision-induced dissociation (CID) tandem mass spectrometry (MS/MS). However, the cleavages of disulfide bonds result in different cysteine modifications in product ions, making it difficult to identify the disulfide-bonded proteins via database search. To solve this identification problem, we have developed a pseudo MS(3) approach by combining nozzle-skimmer dissociation (NSD) and CID on a quadrupole time-of-flight (Q-TOF) mass spectrometer using chicken lysozyme as a model. Although many of the product ions were similar to those typically seen in MS/MS spectra of enzymatically derived peptides, additional uncommon product ions were detected including c(i-1) ions (the i(th) residue being aspartic acid, arginine, lysine and dehydroalanine) as well as those from a scrambled sequence. The formation of these uncommon types of product ions, likely caused by the lack of mobile protons, were proposed to involve bond rearrangements via a six-membered ring transition state and/or salt bridge(s). A search of 20 pseudo MS(3) spectra against the Gallus gallus (chicken) database using Batch-Tag, a program originally designed for bottom up MS/MS analysis, identified chicken lysozyme as the only hit with the expectation values less than 0.02 for 12 of the spectra. The pseudo MS(3) approach may help to identify disulfide-bonded proteins and determine the associated post-translational modifications (PTMs); the confidence in the identification may be improved by incorporating the fragmentation characteristics into currently available search programs.
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