Top‐down analysis of novel synthetic branched proteins
Open accessAbstract
A strategy for top‐down analysis of branched proteins has been reported earlier, which relies on electron transfer dissociation assisted by collisional activation, and software designed for graphic interpretation of tandem mass spectra and adapted for branched proteins. In the present study, the strategy is applied to identify unknown and novel products of reactions in which rationally mutated proteoforms of Rub1 are used to probe the selectivity of E1 and E2 enzymes normally active in ubiquitination. To test and demonstrate this application, components and attachment sites of three branched dimers are deduced and the mutations are confirmed.
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TDMS is well suited for identifying and characterizing branched systems consisting of two proteins.
“In addition, as demonstrated by Gomes and co-workers33,34, TDMS is well-suited for identification and characterization of branched systems consisting of two proteins.”
From Recent trends of capillary electrophoresis‐mass spectrometry in proteomics research (2019) · cites this paper as [33]
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- Authors
- Gomes, F., Lemma, B., Abeykoon, D., Chen, D., Wang, Y., Fushman, D., & Fenselau, C.
- Affiliations
- Department of Chemistry and Biochemistry University of Maryland College Park MD 20742 USA
- University of Maryland, College Park (US)
- Corresponding author
- Fushman, David
- Fenselau, Catherine
- Venue
- Journal of Mass Spectrometry
- Publisher
- Wiley
- Published
- 2018-12-13
- Volume
- 54
- Issue
- 1
- Pages
- 19-25
- ISSN
- 1076-5174 (ISSN-L)
- 1096-9888
- PMC
- PMC7236025
- OpenAlex
- W2897196406
- Cited by
- 7
- References
- 19
- Citations by year
- 2022: 2 · 2021: 1 · 2020: 1 · 2019: 3
- FWCI
- 0.54
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of Mass Spectrometry (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation (MCB1818280)
- Foundation for the National Institutes of Health (GM021248, OD019938)
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- top-down mass spectrometry, electron transfer dissociation, collisional activation, proteoforms, ubiquitination
- MeSH terms
- Chromatography, High Pressure Liquid, Electron Transport, Ubiquitin, Tandem Mass Spectrometry, Ubiquitination
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