ArticleJournal of the American Society for Mass Spectrometry2009
Shifting unoccupied spectral space in mass spectrum of peptide fragment ions.
Article in Journal of the American Society for Mass Spectrometry, 2009. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 10 citations in OpenAlex.
- Iodine-Containing Mass-Defect-Tuned Dendrimers for Use as Internal Mass Spectrometry Calibrants.Journal of the American Society for Mass Spectrometry · 2018Article
- Article
- Identification of Phosphorylated Human Peptides by Accurate Mass Measurement Alone.International journal of mass spectrometry · 2011Article
- Drug metabolite profiling and identification by high-resolution mass spectrometry.The Journal of biological chemistry · 2011Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ions near the high-end border of a mass defect distribution plot for native peptide fragment ions have potential as signature markers that are based on mass-to-charge ratio determination. The specificity of these marker ions, including phosphoryl ions, can be improved by removing interfering isobaric ions from the border region on the distribution plot. These interfering ions are rich in Asp and Glu content. The masses of amino acid residues and peptides are rescaled from the IUPAC scale (12C = 12 u as the mass reference) to the averagine scale (averagine mass = 111 u* as the mass reference with zero mass defect; u*: the mass unit on the averagine scale), using a scaling factor of 0.999493894. It is theoretically predicted that esterification of Asp and Glu side-chain carboxylates with n-butanol can achieve a sufficient retreat of the high-end border on a mass defect distribution plot based on the use of mass spectrometers with better-than-medium resolution. Theoretical calculations and laboratory experiments are performed to examine effects of various esterifications on the averagine-scale mass defect distribution of peptide fragment ions and on the specificity of two positive phosphoryl ions: the phosphotyrosine immonium ion and a cyclophosphoramidate ion.
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Registered trials
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