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MS3 for peptide identification and mapping phosphorylation sites

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Presentation on theme: "MS3 for peptide identification and mapping phosphorylation sites"— Presentation transcript:

1 MS3 for peptide identification and mapping phosphorylation sites
MS3 for peptide identification and mapping phosphorylation sites.A, MS2 fragmentation (parent ion m/z, ) of phosphopeptide IQELKGpSQER (where pS is phosphoserine) (carboxylesterase 5, gi|Mb ) shows a dominant neutral loss peak at m/z and few fragment masses providing sequence information. MS3 for peptide identification and mapping phosphorylation sites.A, MS2 fragmentation (parent ion m/z, ) of phosphopeptide IQELKGpSQER (where pS is phosphoserine) (carboxylesterase 5, gi|Mb ) shows a dominant neutral loss peak at m/z and few fragment masses providing sequence information. B, MS3 spectrum after fragmentation of the neutral loss peak shows a rich fragmentation pattern for peptide identification and phosphorylation site determination. Asterisks indicate water loss peaks. Jaeick Lee et al. Mol Cell Proteomics 2007;6: © 2007 The American Society for Biochemistry and Molecular Biology

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B. Neutral loss triggered MS3 scan of 983.1, 2+

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14-3-3 binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for 14-3-3 binding. 50 of these correspond.

binding sites 58 of the 473 unambiguously assigned phosphorylation sites are predicted by Scansite to be sites for binding. 50 of these correspond.
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.
MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.

MALDI-TOF MS spectrum of phosphopeptides from plant PM aquaporins.
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 ).
Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.

Phosphorylation and sequence disorder in microtubule-associated protein Tau.A, schematic illustration of the domain profile of Tau with all known phosphorylation.
Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,

Distribution of phosphorylation sites identified in the cytosolic phosphoproteome.A, numbers of approved phosphopeptides, previously phosphorylated peptides,
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 ).
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 ).
Phosphopeptides identified harboring minimal binding motifs

Phosphopeptides identified harboring minimal binding motifs
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
Phosphorylation reduces peptide solution charge state and alters SCX elution at low pH.A, at pH 2.7, a theoretical tryptic peptide without histidine residues.

Phosphorylation reduces peptide solution charge state and alters SCX elution at low pH.A, at pH 2.7, a theoretical tryptic peptide without histidine residues.
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.
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.

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.
Work flow for the LAXIC strategy to quantify the phosphorylation change in response to osmotic stress. Work flow for the LAXIC strategy to quantify the.

Work flow for the LAXIC strategy to quantify the phosphorylation change in response to osmotic stress. Work flow for the LAXIC strategy to quantify the.
Top-down protein identification.

Top-down protein identification.

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