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.

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Legends For ETD data In the spectra  = precursor ions, charge-reduced ones too; * = charge-reduced ion from a coeluting precursor ion with different,
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A Phospho-Peptide Spectrum Library for Improved Targeted Assays Barbara Frewen 1, Scott Peterman 1, John Sinclair 2, Claus Jorgensen 2, Amol Prakash 1,
binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.
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Phosphopeptide sequencing by MALDI-TOF/TOF of the C-terminal tail of AtPIP2;4.A, MS/MS spectrum of singly phosphorylated 277ALGSFGSFGSFRSFA291 (m/z ).
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Phosphopeptides identified harboring minimal binding motifs
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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
Frequency distribution of the GRAVY of the theoretical proteins (open bars) and of 110 genes encoding proteins identified on a 2-D electrophoresis gel,
Beam-type (Q-TOF) CID data of m/z (3+).
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.
MS spectra of intact histones (A) and peptides 1–41 (B) of the second H2A HPLC peak.A, molecular masses of intact histones H2A determined after deconvolution.
Top-down protein identification.
Schematic of MS1 filtering.
Significantly enriched phosphorylation motifs from up-regulated phosphopeptides by Motif-X analysis. Significantly enriched phosphorylation motifs from.
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N-terminal extension of a gene using peptides mapping upstream to an annotated start site. N-terminal extension of a gene using peptides mapping upstream.
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MS/MS spectra of INEILSNALKR with a Lys residue modified with SUMO1 or SUMO3 remnant chains. MS/MS spectra of INEILSNALKR with a Lys residue modified with.
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Interaction networks of the regulated phosphoproteins.
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SDS-PAGE of IGFBP-5 from 32P-labeled T47D cells and separation of tryptic phosphopeptides separated by HPLC.a, an autoradiograph (lane 1) is shown next.
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Tryptic glycopeptides of IGFBP-5 from T47D cells separated by HPLC detected by ESI-MS and sequenced by tandem MS.a, ESI-MS spectrum of combined fractions.
Full-length AdIGFBP-5 and T47D cell-derived IGFBP-5 analyzed by mass spectrometry.a, intact AdIGFBP-5 was analyzed by ESI-MS. Full-length AdIGFBP-5 and.
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Phosphopeptides identified harboring minimal binding motifs
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MS3 for peptide identification and mapping phosphorylation sites
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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 of m/z 624.950(3+), acquired on a Orbitrap Fusion Lumos Tribrid mass spectrometer (Thermo Fisher Scientific) (at NCE = 15%). The modified sequence was identified from these data as AVAVTLQSH [342–350] of human YIPF3 protein (Uniprot ID: Q9GZM5). The glycan is most likely the disialo mucin-type core-1 structure, one of the glycans listed as potential variable modifications of Ser and Thr residues. Extensive HexNAc fragmentation was not observed, thus, the GalNAc's identity cannot be established unambiguously from these data. In the reducing end fragment ion Y2SA, the sialic acid could be linked either to the GalNAc or the Gal. The modification site was identified as Thr-5, fragments printed in red are unique to this positional variant. No fragment ions indicated modification on the Ser residue. The precursor ion and its charge-reduced versions are labeled as “pr.” Zsuzsanna Darula, and Katalin F. Medzihradszky Mol Cell Proteomics 2018;17:2-17 © 2018 by The American Society for Biochemistry and Molecular Biology, Inc.