Presentation is loading. Please wait.

Presentation is loading. Please wait.

2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj

Published by정비 금 Modified over 5 years ago

Similar presentations

Presentation on theme: "2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj"— Presentation transcript:

1 2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj
2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj.) using DIA and targeted identification with an inclusion list. 2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj.) using DIA and targeted identification with an inclusion list.A, BPC, B, XIC for m/z , C, extracted fragment ion spectrum (precursor isolation window of m/z 950 ± 50) from which the mass of the SUMO3 peptide candidate was calculated to be Da based on the observation of the [M+3H]3+ ion at m/z for the peak eluting at 34.5 min. D, MS/MS spectrum (30 V collision energy) from the targeted analysis of [M+3H]3+ at m/z confirming the sequence of the SUMO3 peptide as ATGDETGAK(NQTGG)VERADGYEPPVQESV corresponding to 40S ribosomal protein S3a with a modified K249 residue. Frederic Lamoliatte et al. Mol Cell Proteomics 2013;12: © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.

Download ppt "2D-LC-MS/MS analysis of tryptic digest of HEK293-SUMO3 cells (2 μg inj"

Similar presentations

Sequence alignment of C-terminal phosphorylated plant aquaporins

Sequence alignment of C-terminal phosphorylated plant aquaporins
Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.

Principle for quantification of phosphorylation of the C-terminal tail of AtPIP2;1. Principle for quantification of phosphorylation of the C-terminal tail.
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z 1188.53).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;1.A, MS/MS spectrum of singly phosphorylated 277SLGSFRSAANV287 (m/z ).
Experimental overview A sequential protein and peptide IMAC enrichment was analyzed by four different LC-MS/MS strategies. Experimental overview A sequential.

Experimental overview A sequential protein and peptide IMAC enrichment was analyzed by four different LC-MS/MS strategies. Experimental overview A sequential.
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z 1617.55).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
Proteomics Informatics David Fenyő

Proteomics Informatics David Fenyő
Fast protein LC IMAC purification of cytosolic phosphoproteins

Fast protein LC IMAC purification of cytosolic phosphoproteins
Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z 1217.53).

Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;7.A, MS/MS spectrum of singly phosphorylated 270ALGSFRSNATN280 (m/z ).
Proteomics Informatics –

Proteomics Informatics –
A quantitative proteomics strategy to identify SUMO-conjugated proteins. A quantitative proteomics strategy to identify SUMO-conjugated proteins. HeLa.

A quantitative proteomics strategy to identify SUMO-conjugated proteins. A quantitative proteomics strategy to identify SUMO-conjugated proteins. HeLa.
Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.

Percentage of proteins identified in envelope membrane extracts according to the purification method and the number of transmembrane domains. Percentage.
Novel phosphorylation sites on H+-ATPase proteins

Novel phosphorylation sites on H+-ATPase proteins
MIDAS workflow000000 (MRM-triggered MS/MS) verification of the identity of peptide DLQFVEVTDVK representing fibronectin (normal concentration, ∼300 μg/ml)

MIDAS workflow (MRM-triggered MS/MS) verification of the identity of peptide DLQFVEVTDVK representing fibronectin (normal concentration, ∼300 μg/ml)
A, high resolution MS/MS spectrum (lower panel) of 1435

A, high resolution MS/MS spectrum (lower panel) of 1435
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,

Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
EThcD spectrum of m/z 624.950(3+), acquired on a Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific) (at NCE = 15%). EThcD spectrum.

EThcD spectrum of m/z (3+), acquired on a Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific) (at NCE = 15%). EThcD spectrum.
Relative quantitation of phosphopeptides from conditioned media from subtype specific breast cancer cell lines. Relative quantitation of phosphopeptides.

Relative quantitation of phosphopeptides from conditioned media from subtype specific breast cancer cell lines. Relative quantitation of phosphopeptides.
Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.

Time course of phosphorylation changes at Ser-293, Ser-300, and Ser-232 in PDHE1α following kinase inhibition with DCA. A, relative quantitation over three.
Top-down protein identification.

Top-down protein identification.
Schematic of MS1 filtering.

Schematic of MS1 filtering.

Similar presentations

Ads by Google