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Automatic internal calibration in liquid chromatography/Fourier transform ion cyclotron resonance mass spectrometry of protein digests

Palmblad, M., Bindschedler, L.V., Gibson, T. M. and Cramer, R. (2006) Automatic internal calibration in liquid chromatography/Fourier transform ion cyclotron resonance mass spectrometry of protein digests. Rapid Communications in Mass Spectrometry, 20 (20). pp. 3076-3080. ISSN 0951-4198

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To link to this article DOI: 10.1002/rcm.2707

Abstract/Summary

Accurately measured peptide masses can be used for large-scale protein identification from bacterial whole-cell digests as an alternative to tandem mass spectrometry (MS/MS) provided mass measurement errors of a few parts-per-million (ppm) are obtained. Fourier transform ion cyclotron resonance (FTICR) mass spectrometry (MS) routinely achieves such mass accuracy either with internal calibration or by regulating the charge in the analyzer cell. We have developed a novel and automated method for internal calibration of liquid chromatography (LC)/FTICR data from whole-cell digests using peptides in the sample identified by concurrent MS/MS together with ambient polydimethyl-cyclosiloxanes as internal calibrants in the mass spectra. The method reduced mass measurement error from 4.3 +/- 3.7 ppm to 0.3 +/- 2.3 ppm in an E. coli LC/FTICR dataset of 1000 MS and MS/MS spectra and is applicable to all analyses of complex protein digests by FTICRMS. Copyright (c) 2006 John Wiley & Sons, Ltd.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:11546
Uncontrolled Keywords:ACCURATE MASS, POSTTRANSLATIONAL MODIFICATIONS, IDENTIFICATION, PROTEOMICS, PREDICTION, TAGS

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