The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Improved peptide identification in proteomics by two consecutive stages of mass spectrometric fragmentation
Open accessAbstract
MS-based proteomics usually involves the fragmentation of tryptic peptides (tandem MS or MS 2 ) and their identification by searching protein sequence databases. In ion trap instruments fragments can be further fragmented and analyzed, a process termed MS/MS/MS or MS 3 . Here, we report that efficient ion capture in a linear ion trap leads to MS 3 acquisition times and spectra quality similar to those for MS 2 experiments with conventional 3D ion traps. Fragmentation of N- or C-terminal ions resulted in informative and low-background spectra, even at subfemtomol levels of peptide. Typically C-terminal ions are chosen for further fragmentation, and the MS 3 spectrum greatly constrains the C-terminal amino acids of the peptide sequence. MS 3 spectra allow resolution of ambiguities in identification, a crucial problem in proteomics. Because of the sensitivity and rapid scan rates of the linear ion trap, several MS 3 spectra per peptide can be obtained even when sequencing very complex mixtures. We calculate the probability that an experimental MS 3 spectrum originates from fragmentation of a given N- or C-terminal ion of a peptide under consideration. This MS 3 identification score can be combined with the MS 2 scores of the precursor peptide from existing search engines. When MS 3 is performed on the linear ion trap–Fourier transform mass spectrometer combination, accurate peptide masses further increase confidence in peptide identification.
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Self-citationMass spectrometry-based proteomics
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A Statistical Model for Identifying Proteins by Tandem Mass Spectrometry
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Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Self-citationUniversal sample preparation method for proteome analysis
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Self-citationIn-gel digestion for mass spectrometric characterization of proteins and proteomes
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Self-citationProtein biomarker discovery and validation: the long and uncertain path to clinical utility
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Protein Analysis by Shotgun/Bottom-up Proteomics
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Metadata
- Authors
- Olsen, J. V., & Mann, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2004-09-03
- Volume
- 101
- Issue
- 37
- Pages
- 13417-13422
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2062049401
- Cited by
- 313
- References
- 28
- FWCI
- 14.09
- Type
- journal article
- Language
- en
- Open access
- green
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