Electron capture dissociation of singly and multiply phosphorylated peptides

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Electron capture dissociation of singly and multiply phosphorylated peptides. / Stensballe, A; Jensen, Ole Nørregaard; Olsen, Jesper Velgaard; Haselmann, K F; Zubarev, R A.

In: Rapid Communications in Mass Spectrometry, Vol. 14, No. 19, 2000, p. 1793-800.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Stensballe, A, Jensen, ON, Olsen, JV, Haselmann, KF & Zubarev, RA 2000, 'Electron capture dissociation of singly and multiply phosphorylated peptides', Rapid Communications in Mass Spectrometry, vol. 14, no. 19, pp. 1793-800. https://doi.org/10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q

APA

Stensballe, A., Jensen, O. N., Olsen, J. V., Haselmann, K. F., & Zubarev, R. A. (2000). Electron capture dissociation of singly and multiply phosphorylated peptides. Rapid Communications in Mass Spectrometry, 14(19), 1793-800. https://doi.org/10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q

Vancouver

Stensballe A, Jensen ON, Olsen JV, Haselmann KF, Zubarev RA. Electron capture dissociation of singly and multiply phosphorylated peptides. Rapid Communications in Mass Spectrometry. 2000;14(19):1793-800. https://doi.org/10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q

Author

Stensballe, A ; Jensen, Ole Nørregaard ; Olsen, Jesper Velgaard ; Haselmann, K F ; Zubarev, R A. / Electron capture dissociation of singly and multiply phosphorylated peptides. In: Rapid Communications in Mass Spectrometry. 2000 ; Vol. 14, No. 19. pp. 1793-800.

Bibtex

@article{471a0390eb0311deba73000ea68e967b,
title = "Electron capture dissociation of singly and multiply phosphorylated peptides",
abstract = "Analysis of phosphotyrosine and phosphoserine containing peptides by nano-electrospray Fourier transform ion cyclotron resonance (FTICR) mass spectrometry established electron capture dissociation (ECD) as a viable method for phosphopeptide sequencing. In general, ECD spectra of synthetic and native phosphopeptides appeared less complex than conventional collision activated dissociation (CAD) mass spectra of these species. ECD of multiply protonated phosphopeptide ions generated mainly c- and z(.)-type peptide fragment ion series. No loss of water, phosphate groups or phosphoric acid from intact phosphopeptide ions nor from the c and z(.) fragment ion products was observed in the ECD spectra. ECD enabled complete or near-complete amino acid sequencing of phosphopeptides for the assignment of up to four phosphorylation sites in peptides in the mass range 1400 to 3500 Da. Nano-scale Fe(III)-affinity chromatography combined with nano-electrospray FTMS/ECD facilitated phosphopeptide analysis and amino acid sequencing from crude proteolytic peptide mixtures.",
author = "A Stensballe and Jensen, {Ole N{\o}rregaard} and Olsen, {Jesper Velgaard} and Haselmann, {K F} and Zubarev, {R A}",
note = "Keywords: Amino Acid Sequence; Animals; Caseins; Cattle; Chromatography, Affinity; Fourier Analysis; Mass Spectrometry; Molecular Sequence Data; Phosphopeptides; Phosphorylation; Phosphoserine; Phosphotyrosine",
year = "2000",
doi = "10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q",
language = "English",
volume = "14",
pages = "1793--800",
journal = "Rapid Communications in Mass Spectrometry",
issn = "0951-4198",
publisher = "JohnWiley & Sons Ltd",
number = "19",

}

RIS

TY - JOUR

T1 - Electron capture dissociation of singly and multiply phosphorylated peptides

AU - Stensballe, A

AU - Jensen, Ole Nørregaard

AU - Olsen, Jesper Velgaard

AU - Haselmann, K F

AU - Zubarev, R A

N1 - Keywords: Amino Acid Sequence; Animals; Caseins; Cattle; Chromatography, Affinity; Fourier Analysis; Mass Spectrometry; Molecular Sequence Data; Phosphopeptides; Phosphorylation; Phosphoserine; Phosphotyrosine

PY - 2000

Y1 - 2000

N2 - Analysis of phosphotyrosine and phosphoserine containing peptides by nano-electrospray Fourier transform ion cyclotron resonance (FTICR) mass spectrometry established electron capture dissociation (ECD) as a viable method for phosphopeptide sequencing. In general, ECD spectra of synthetic and native phosphopeptides appeared less complex than conventional collision activated dissociation (CAD) mass spectra of these species. ECD of multiply protonated phosphopeptide ions generated mainly c- and z(.)-type peptide fragment ion series. No loss of water, phosphate groups or phosphoric acid from intact phosphopeptide ions nor from the c and z(.) fragment ion products was observed in the ECD spectra. ECD enabled complete or near-complete amino acid sequencing of phosphopeptides for the assignment of up to four phosphorylation sites in peptides in the mass range 1400 to 3500 Da. Nano-scale Fe(III)-affinity chromatography combined with nano-electrospray FTMS/ECD facilitated phosphopeptide analysis and amino acid sequencing from crude proteolytic peptide mixtures.

AB - Analysis of phosphotyrosine and phosphoserine containing peptides by nano-electrospray Fourier transform ion cyclotron resonance (FTICR) mass spectrometry established electron capture dissociation (ECD) as a viable method for phosphopeptide sequencing. In general, ECD spectra of synthetic and native phosphopeptides appeared less complex than conventional collision activated dissociation (CAD) mass spectra of these species. ECD of multiply protonated phosphopeptide ions generated mainly c- and z(.)-type peptide fragment ion series. No loss of water, phosphate groups or phosphoric acid from intact phosphopeptide ions nor from the c and z(.) fragment ion products was observed in the ECD spectra. ECD enabled complete or near-complete amino acid sequencing of phosphopeptides for the assignment of up to four phosphorylation sites in peptides in the mass range 1400 to 3500 Da. Nano-scale Fe(III)-affinity chromatography combined with nano-electrospray FTMS/ECD facilitated phosphopeptide analysis and amino acid sequencing from crude proteolytic peptide mixtures.

U2 - 10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q

DO - 10.1002/1097-0231(20001015)14:19<1793::AID-RCM95>3.0.CO;2-Q

M3 - Journal article

C2 - 11006587

VL - 14

SP - 1793

EP - 1800

JO - Rapid Communications in Mass Spectrometry

JF - Rapid Communications in Mass Spectrometry

SN - 0951-4198

IS - 19

ER -

ID: 16330710