Proteomics

Dataset Information

0

Electron Transfer/ Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations


ABSTRACT: Fragmentation behaviour of labile phosphorylated peptides

INSTRUMENT(S): Orbitrap Fusion ETD

ORGANISM(S): Bos Taurus (bovine) Homo Sapiens (human) Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Martin Penkert  

LAB HEAD: Eberhard Krause

PROVIDER: PXD012989 | Pride | 2019-05-27

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
EThcD.xlsx Xlsx
MP13_Pyro_doubly_charged_EThcD30.mgf Mgf
MP13_Pyro_doubly_charged_EThcD30.msf Msf
MP13_Pyro_doubly_charged_EThcD30.msfView Msf
MP13_Pyro_doubly_charged_EThcD30.pdResult Other
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Publications

Electron Transfer/Higher Energy Collisional Dissociation of Doubly Charged Peptide Ions: Identification of Labile Protein Phosphorylations.

Penkert Martin M   Hauser Anett A   Harmel Robert R   Fiedler Dorothea D   Hackenberger Christian P R CPR   Krause Eberhard E  

Journal of the American Society for Mass Spectrometry 20190520 9


In recent years, labile phosphorylation sites on arginine, histidine, cysteine, and lysine as well as pyrophosphorylation of serine and threonine have gained more attention in phosphoproteomic studies. However, the analysis of these delicate posttranslational modifications via tandem mass spectrometry remains a challenge. Common fragmentation techniques such as collision-induced dissociation (CID) and higher energy collisional dissociation (HCD) are limited due to extensive phosphate-related neu  ...[more]

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