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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

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			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]

PMID: 31111417

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