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  A large synthetic peptide and phosphopeptide reference library for mass spectrometry-based proteomics

Marx, H., Lemeer, S., Schliep, J. E., Matheron, L., Mohammed, S., Cox, J., et al. (2013). A large synthetic peptide and phosphopeptide reference library for mass spectrometry-based proteomics. NATURE BIOTECHNOLOGY, 31(6), 557-564. doi:10.1038/nbt.2585.

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 Urheber:
Marx, Harald1, Autor
Lemeer, Simone1, Autor
Schliep, Jan Erik1, Autor
Matheron, Lucrece1, Autor
Mohammed, Shabaz1, Autor
Cox, Juergen2, Autor           
Mann, Matthias2, Autor           
Heck, Albert J. R.1, Autor
Kuster, Bernhard1, Autor
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

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Schlagwörter: PHOSPHORYLATION SITE LOCALIZATION; PROTEIN IDENTIFICATION; SHOTGUN PROTEOMICS; STATISTICAL-MODEL; MS/MS; FRAGMENTATION; SPECTRA; PHOSPHOPROTEOMICS; PREDICTION; SEARCH
 Zusammenfassung: We present a peptide library and data resource of > 100,000 synthetic, unmodified peptides and their phosphorylated counterparts with known sequences and phosphorylation sites. Analysis of the library by mass spectrometry yielded a data set that we used to evaluate the merits of different search engines (Mascot and Andromeda) and fragmentation methods (beam-type collision-induced dissociation (HCD) and electron transfer dissociation (ETD)) for peptide identification. We also compared the sensitivities and accuracies of phosphorylation-site localization tools (Mascot Delta Score, PTM score and phosphoRS), and we characterized the chromatographic behavior of peptides in the library. We found that HCD identified more peptides and phosphopeptides than did ETD, that phosphopeptides generally eluted later from reversed-phase columns and were easier to identify than unmodified peptides and that current computational tools for proteomics can still be substantially improved. These peptides and spectra will facilitate the development, evaluation and improvement of experimental and computational proteomic strategies, such as separation techniques and the prediction of retention times and fragmentation patterns.

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Sprache(n): eng - English
 Datum: 2013-06
 Publikationsstatus: Erschienen
 Seiten: 8
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: ISI: 000320113200029
DOI: 10.1038/nbt.2585
 Art des Abschluß: -

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Titel: NATURE BIOTECHNOLOGY
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Seiten: - Band / Heft: 31 (6) Artikelnummer: - Start- / Endseite: 557 - 564 Identifikator: ISSN: 1087-0156