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Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy.

Research output: Contribution to journalJournal article

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Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy. / Hart, Sarah R.; Wai Lau, King Wai; Hao, Zhiqi; Broadhead, Richard; Portman, Neil; Huhmer, Andreas; Gull, Keith; McKean, Paul G.; Hubbard, Simon J.; Gaskell, Simon J.

In: Journal of The American Society for Mass Spectrometry, Vol. 20, No. 2, 02.2009, p. 167-175.

Research output: Contribution to journalJournal article

Harvard

Hart, SR, Wai Lau, KW, Hao, Z, Broadhead, R, Portman, N, Huhmer, A, Gull, K, McKean, PG, Hubbard, SJ & Gaskell, SJ 2009, 'Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy.', Journal of The American Society for Mass Spectrometry, vol. 20, no. 2, pp. 167-175. https://doi.org/10.1016/j.jasms.2008.08.014

APA

Hart, S. R., Wai Lau, K. W., Hao, Z., Broadhead, R., Portman, N., Huhmer, A., ... Gaskell, S. J. (2009). Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy. Journal of The American Society for Mass Spectrometry, 20(2), 167-175. https://doi.org/10.1016/j.jasms.2008.08.014

Vancouver

Hart SR, Wai Lau KW, Hao Z, Broadhead R, Portman N, Huhmer A et al. Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy. Journal of The American Society for Mass Spectrometry. 2009 Feb;20(2):167-175. https://doi.org/10.1016/j.jasms.2008.08.014

Author

Hart, Sarah R. ; Wai Lau, King Wai ; Hao, Zhiqi ; Broadhead, Richard ; Portman, Neil ; Huhmer, Andreas ; Gull, Keith ; McKean, Paul G. ; Hubbard, Simon J. ; Gaskell, Simon J. / Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy. In: Journal of The American Society for Mass Spectrometry. 2009 ; Vol. 20, No. 2. pp. 167-175.

Bibtex

@article{d2984ac15fd043b1b2e496c32120fcca,
title = "Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy.",
abstract = "The use of electron-transfer dissociation as an alternative peptide ion activation method for generation of protein sequence information is examined here in comparison with the conventional method of choice, collisionally activated dissociation, using a linear ion trapping instrument. Direct comparability between collisionally and electron-transfer-activated product ion data were ensured by employing an activation-switching method during acquisition, sequentially activating precisely the same precursor ion species with each fragmentation method in turn. Sequest (Thermo Fisher Scientific, San Jose, CA) searching of product ion data generated an overlapping yet distinct pool of polypeptide identifications from the products of collisional and electron-transfer-mediated activation products. To provide a highly confident set of protein recognitions, identification data were filtered using parameters that achieved a peptide false discovery rate of 1{\%}, with two or more independent peptide assignments required for each protein. The use of electron transfer dissociation (ETD) has allowed us to identify additional peptides where the quality of product ion data generated by collisionally activated dissociation (CAD) was insufficient to infer peptide sequence. Thus, a combined ETD/CAD approach leads to the recognition of more peptides and proteins than are achieved using peptide analysis by CAD- or ETD-based tandem mass spectrometry alone.",
author = "Hart, {Sarah R.} and {Wai Lau}, {King Wai} and Zhiqi Hao and Richard Broadhead and Neil Portman and Andreas Huhmer and Keith Gull and McKean, {Paul G.} and Hubbard, {Simon J.} and Gaskell, {Simon J.}",
year = "2009",
month = "2",
doi = "10.1016/j.jasms.2008.08.014",
language = "English",
volume = "20",
pages = "167--175",
journal = "Journal of The American Society for Mass Spectrometry",
issn = "1044-0305",
publisher = "Springer New York",
number = "2",

}

RIS

TY - JOUR

T1 - Analysis of the trypanosome flagellar proteome using a combined electron transfer collisionally activated dissociation strategy.

AU - Hart, Sarah R.

AU - Wai Lau, King Wai

AU - Hao, Zhiqi

AU - Broadhead, Richard

AU - Portman, Neil

AU - Huhmer, Andreas

AU - Gull, Keith

AU - McKean, Paul G.

AU - Hubbard, Simon J.

AU - Gaskell, Simon J.

PY - 2009/2

Y1 - 2009/2

N2 - The use of electron-transfer dissociation as an alternative peptide ion activation method for generation of protein sequence information is examined here in comparison with the conventional method of choice, collisionally activated dissociation, using a linear ion trapping instrument. Direct comparability between collisionally and electron-transfer-activated product ion data were ensured by employing an activation-switching method during acquisition, sequentially activating precisely the same precursor ion species with each fragmentation method in turn. Sequest (Thermo Fisher Scientific, San Jose, CA) searching of product ion data generated an overlapping yet distinct pool of polypeptide identifications from the products of collisional and electron-transfer-mediated activation products. To provide a highly confident set of protein recognitions, identification data were filtered using parameters that achieved a peptide false discovery rate of 1%, with two or more independent peptide assignments required for each protein. The use of electron transfer dissociation (ETD) has allowed us to identify additional peptides where the quality of product ion data generated by collisionally activated dissociation (CAD) was insufficient to infer peptide sequence. Thus, a combined ETD/CAD approach leads to the recognition of more peptides and proteins than are achieved using peptide analysis by CAD- or ETD-based tandem mass spectrometry alone.

AB - The use of electron-transfer dissociation as an alternative peptide ion activation method for generation of protein sequence information is examined here in comparison with the conventional method of choice, collisionally activated dissociation, using a linear ion trapping instrument. Direct comparability between collisionally and electron-transfer-activated product ion data were ensured by employing an activation-switching method during acquisition, sequentially activating precisely the same precursor ion species with each fragmentation method in turn. Sequest (Thermo Fisher Scientific, San Jose, CA) searching of product ion data generated an overlapping yet distinct pool of polypeptide identifications from the products of collisional and electron-transfer-mediated activation products. To provide a highly confident set of protein recognitions, identification data were filtered using parameters that achieved a peptide false discovery rate of 1%, with two or more independent peptide assignments required for each protein. The use of electron transfer dissociation (ETD) has allowed us to identify additional peptides where the quality of product ion data generated by collisionally activated dissociation (CAD) was insufficient to infer peptide sequence. Thus, a combined ETD/CAD approach leads to the recognition of more peptides and proteins than are achieved using peptide analysis by CAD- or ETD-based tandem mass spectrometry alone.

UR - http://www.scopus.com/inward/record.url?scp=58249088149&partnerID=8YFLogxK

U2 - 10.1016/j.jasms.2008.08.014

DO - 10.1016/j.jasms.2008.08.014

M3 - Journal article

VL - 20

SP - 167

EP - 175

JO - Journal of The American Society for Mass Spectrometry

JF - Journal of The American Society for Mass Spectrometry

SN - 1044-0305

IS - 2

ER -