The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Cleavage N-Terminal to Proline: Analysis of a Database of Peptide Tandem Mass Spectra
Abstract
Fragmentation at the Xxx-Pro bond was analyzed for a group of peptide mass spectra that were acquired in a Finnigan ion trap mass spectrometer and were generated from proteins digested by enzymes and identified by the Sequest algorithm. Cleavage with formation of a + b + y ions occurred more readily at the Xxx-Pro bond than at other locations in these peptides, and the importance of this cleavage varied by the identity of Xxx. The most abundant Xxx-Pro relative bond cleavage ratios were observed when Xxx was Val, His, Asp, Ile, and Leu, whereas the least abundant cleavage ratios occurred when Xxx was Gly or Pro. Rationalization for these cleavage ratios at Xxx-Pro may include contribution of the Asp or His side chain to enhanced cleavage or the conformation of Pro, Gly, and the aliphatic residues Val, Ile, and Leu at the Xxx location in the Xxx-Pro bond. Although unusual fragmentation behavior has been noted for Pro-containing peptides, this analysis suggests that fragmentation at the Xxx-Pro bond is predictable and that this information may be used to improve the identification of proteins if it is incorporated into peptide sequencing algorithms.
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Citations
Cites
Matrix-assisted laser desorption/ionization mass spectrometry of biopolymers.
Hillenkamp, F., Karas, M., Beavis, R. C., & Chait, B. T. (1991) · Analytical Chemistry · doi:10.1021/ac00024a716 · Cited by 1,930
Influence of proline residues on protein conformation
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Cited by
Rauniyar, N. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161226120 · Cited by 406
“Also, in case of proline-containing peptides, fragmentation at the N-terminal side of proline residue in a mass spectrometer generates an intense fragment ion; the fragment ion peak is dramatically over-represented in the MS/MS spectra (Figure 2a) [33].”
BackgroundProteomics of Integral Membrane ProteinsTheory and Application
Speers, A. E., & Wu, C. C. (2007) · Chemical Reviews · doi:10.1021/cr068286z · Cited by 325
Welker, F., Hajdinjak, M., Talamo, S., Jaouen, K., Dannemann, M., David, F., Julien, M., Meyer, M., Kelso, J., Barnes, I., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605834113 · Cited by 309
A guide to ancient protein studies
Hendy, J., Welker, F., Demarchi, B., Speller, C., Warinner, C., & Collins, M. J. (2018) · Nature Ecology & Evolution · doi:10.1038/s41559-018-0510-x · Cited by 291
Li, H., Nguyen, H. H., Ogorzalek Loo, R. R., Campuzano, I. D. G., & Loo, J. A. (2018) · Nature Chemistry · doi:10.1038/nchem.2908 · Cited by 249
Metadata
- Authors
- Breci, L. A., Tabb, D. L., Yates, J. R., & Wysocki, V. H.
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2003-03-27
- Volume
- 75
- Issue
- 9
- Pages
- 1963-1971
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2055934103
- Cited by
- 312
- References
- 2
- FWCI
- 12.27
- Type
- journal article
- Language
- en
- Open access
- closed
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- Breci, L. A., Tabb, D. L., Yates, J. R., & Wysocki, V. H. (2003). Cleavage N-Terminal to Proline: Analysis of a Database of Peptide Tandem Mass Spectra. Analytical Chemistry. https://doi.org/10.1021/ac026359i
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