Proteomics

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Ultraviolet Photodissociation of tryptic peptide backbones at 213 nm


ABSTRACT: We analyzed the backbone fragmentation behavior of tryptic peptides of a four protein mixture and of E. coli lysate subjected to Ultraviolet Photodissociation (UVPD) at 213 nm on a commercially available UVPD-equipped tribrid mass spectrometer. We obtained 15,178 high-confidence peptide-spectrum matches by additionally recording a reference beam-type collision-induced dissociation (HCD) spectrum of each precursor. Type a, b and y ions were most prominent in UVPD spectra and median sequence coverage ranged from 5.8% (at 5 ms laser excitation time) to 45.0% (at 100 ms). Overall sequence fragment intensity remained relatively low (median: 0.4% (5 ms) to 16.8% (100 ms) of total intensity) and remaining precursor intensity high. Sequence coverage and sequence fragment intensity ratio correlated with precursor charge density, suggesting that UVPD at 213 nm may suffer from newly formed fragments sticking together due to non-covalent interactions. UVPD fragmentation efficiency therefore might benefit from supplemental activation, as was shown for ETD. Aromatic amino acids, most prominently tryptophan, facilitated UVPD. This points at aromatic tags as possible enhancers of UVPD. Data are available via ProteomeXchange and on spectrumviewer.org/db/UVPD_213nm_trypPep

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Equus Caballus (horse) Homo Sapiens (human) Escherichia Coli Gallus Gallus (chicken) Oryctolagus Cuniculus (rabbit)

SUBMITTER: Lars Kolbowski  

LAB HEAD: Juri Rappsilber

PROVIDER: PXD018176 | Pride | 2020-05-07

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
4PM.mzid.gz Mzid
4ProtMix.fasta Fasta
B191105_04_Lumos_AB_DE_165_Ec_dualHCD_HCD_1.raw Raw
B191105_05_Lumos_AB_DE_165_Ec_dualHCD_HCD_2.raw Raw
B191105_07_Lumos_AB_DE_165_4pm_dualHCD_HCD_1.raw Raw
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Publications

Ultraviolet Photodissociation of Tryptic Peptide Backbones at 213 nm.

Kolbowski Lars L   Belsom Adam A   Rappsilber Juri J  

Journal of the American Society for Mass Spectrometry 20200522 6


We analyzed the backbone fragmentation behavior of tryptic peptides of a four-protein mixture and of <i>E. coli</i> lysate subjected to ultraviolet photodissociation (UVPD) at 213 nm on a commercially available UVPD-equipped tribrid mass spectrometer. We obtained 15 178 unique high-confidence peptide UVPD spectrum matches by recording a reference beam-type collision-induced dissociation (HCD) spectrum of each precursor, ensuring that our investigation includes a broad selection of peptides, incl  ...[more]

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