Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS

Steven M. Patrie, Jay Charlebois, Derek Vander Molen, Fanyu Meng, Andrew Forbes, John P. Quinn, Christopher L. Hendrickson, Alan G. Marshall, Neil L. Kelleher

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Abstract

The Proteomics of methanococcus jannaschii and saccharomyces cerevisiae were studied using a quadrupole FT-ICR-MS. It was found that the top down approach fragments intact proteins within the mass spectrometer, which allowed more sequence coverage. It was shown that the micro-electrosprayed ion was desolvated and transported for accumulation either by placing the quadrupole in rf-only or mass filtered by quadrupole. Analysis shows that post transcription processing events increased proteome complexity which ultimately increased the database complexity for larger proteins in higher order organisms.

Original languageEnglish (US)
Title of host publicationProceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics
Pages687-688
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

Fingerprint

Yeast
Mass spectrometers
Proteome
Transcription
Proteins
Ions
Processing
Proteomics

ASJC Scopus subject areas

  • Spectroscopy

Cite this

Patrie, S. M., Charlebois, J., Vander Molen, D., Meng, F., Forbes, A., Quinn, J. P., ... Kelleher, N. L. (2002). Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics (pp. 687-688)

Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS. / Patrie, Steven M.; Charlebois, Jay; Vander Molen, Derek; Meng, Fanyu; Forbes, Andrew; Quinn, John P.; Hendrickson, Christopher L.; Marshall, Alan G.; Kelleher, Neil L.

Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. 2002. p. 687-688.

Research output: Chapter in Book/Report/Conference proceedingConference contribution

Patrie, SM, Charlebois, J, Vander Molen, D, Meng, F, Forbes, A, Quinn, JP, Hendrickson, CL, Marshall, AG & Kelleher, NL 2002, Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS. in Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. pp. 687-688, Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States, 6/2/02.
Patrie SM, Charlebois J, Vander Molen D, Meng F, Forbes A, Quinn JP et al. Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS. In Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. 2002. p. 687-688
Patrie, Steven M. ; Charlebois, Jay ; Vander Molen, Derek ; Meng, Fanyu ; Forbes, Andrew ; Quinn, John P. ; Hendrickson, Christopher L. ; Marshall, Alan G. ; Kelleher, Neil L. / Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS. Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics. 2002. pp. 687-688
@inproceedings{ab442c1ce0ea4df1bf12ced2e4bdfbdd,
title = "Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS",
abstract = "The Proteomics of methanococcus jannaschii and saccharomyces cerevisiae were studied using a quadrupole FT-ICR-MS. It was found that the top down approach fragments intact proteins within the mass spectrometer, which allowed more sequence coverage. It was shown that the micro-electrosprayed ion was desolvated and transported for accumulation either by placing the quadrupole in rf-only or mass filtered by quadrupole. Analysis shows that post transcription processing events increased proteome complexity which ultimately increased the database complexity for larger proteins in higher order organisms.",
author = "Patrie, {Steven M.} and Jay Charlebois and {Vander Molen}, Derek and Fanyu Meng and Andrew Forbes and Quinn, {John P.} and Hendrickson, {Christopher L.} and Marshall, {Alan G.} and Kelleher, {Neil L.}",
year = "2002",
language = "English (US)",
pages = "687--688",
booktitle = "Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics",

}

TY - GEN

T1 - Strategies for top-down proteomics of Methanococcus jannaschii and Saccharomyces cerevisiae using a quadrupole FT-ICR-MS

AU - Patrie, Steven M.

AU - Charlebois, Jay

AU - Vander Molen, Derek

AU - Meng, Fanyu

AU - Forbes, Andrew

AU - Quinn, John P.

AU - Hendrickson, Christopher L.

AU - Marshall, Alan G.

AU - Kelleher, Neil L.

PY - 2002

Y1 - 2002

N2 - The Proteomics of methanococcus jannaschii and saccharomyces cerevisiae were studied using a quadrupole FT-ICR-MS. It was found that the top down approach fragments intact proteins within the mass spectrometer, which allowed more sequence coverage. It was shown that the micro-electrosprayed ion was desolvated and transported for accumulation either by placing the quadrupole in rf-only or mass filtered by quadrupole. Analysis shows that post transcription processing events increased proteome complexity which ultimately increased the database complexity for larger proteins in higher order organisms.

AB - The Proteomics of methanococcus jannaschii and saccharomyces cerevisiae were studied using a quadrupole FT-ICR-MS. It was found that the top down approach fragments intact proteins within the mass spectrometer, which allowed more sequence coverage. It was shown that the micro-electrosprayed ion was desolvated and transported for accumulation either by placing the quadrupole in rf-only or mass filtered by quadrupole. Analysis shows that post transcription processing events increased proteome complexity which ultimately increased the database complexity for larger proteins in higher order organisms.

UR - http://www.scopus.com/inward/record.url?scp=2442711603&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2442711603&partnerID=8YFLogxK

M3 - Conference contribution

AN - SCOPUS:2442711603

SP - 687

EP - 688

BT - Proceedings 50th ASMS Conference on Mass Spectrometry and Allied Topics

ER -