Formylation of His Residues at Position 2 in Peptide <i>b</i> Ions due to Noncanonical C <sup>α</sup> ‐CO Bond Cleavage: Assignment of the <i>m/z</i> 166 Product Ion in Proteome Data

In peptide sequences containing N-terminus XH motifs, the histidine imidazole side chain facilitates C<sup>α</sup>-CO bond cleavage at residue X.

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Journal
Rapid Communications in Mass Spectrometry
Published
2025-10-23
DOI
https://doi.org/10.1002/rcm.10154
Primary Topic
Mass Spectrometry Techniques and Applications
Type
article
Field-Weighted Citation Impact
0.00

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article

Formylation of His Residues at Position 2 in Peptide b Ions due to Noncanonical C α ‐CO Bond Cleavage: Assignment of the m/z 166 Product Ion in Proteome Data

Marimuthu Vijayasarathy, P. Balaram, Manjunath A. Venkatesha, Sanjeev Kumar
Rapid Communications in Mass Spectrometry
Mass Spectrometry Techniques and Applications
article

Formylation of His Residues at Position 2 in Peptide b Ions due to Noncanonical C α ‐CO Bond Cleavage: Assignment of the m/z 166 Product Ion in Proteome Data

Marimuthu Vijayasarathy, P. Balaram, Manjunath A. Venkatesha, Sanjeev Kumar
article en

Abstract

In peptide sequences containing N-terminus XH motifs, the histidine imidazole side chain facilitates C<sup>α</sup>-CO bond cleavage at residue X.

Rapid Communications in Mass SpectrometryVol. 40(2)
Tata Institute of Fundamental Research (IN), National Centre for Biological Sciences (IN), Propagation Research Associates (United States) (US)
Indian Institute of Science, Jawaharlal Nehru Centre for Advanced Scientific Research, Directorate for Biological Sciences, National Centre for Biological Sciences
Openalex Percentile: Top 72%
Mass Spectrometry Techniques and Applications
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Formylation of His Residues at Position 2 in Peptide <i>b</i> Ions due to Noncanonical C <sup>α</sup> ‐CO Bond Cleavage: Assignment of the <i>m/z</i> 166 Product Ion in Proteome Data — Marimuthu Vijayasarathy, P. Balaram, et al. · Rapid Communications in Mass Spectrometry (2025) | TGRS Research Map | TGRS