期刊
EUROPEAN JOURNAL OF MASS SPECTROMETRY
卷 18, 期 3, 页码 269-277出版社
IM PUBLICATIONS
DOI: 10.1255/ejms.1186
关键词
proteomics; metabolic labeling; calibration; Fourier transform mass spectrometry; accurate mass measurement
资金
- National Science Foundation [CHE-1058913]
- NATIONAL CENTER FOR RESEARCH RESOURCES [R01RR019767] Funding Source: NIH RePORTER
High mass measurement accuracy of peptides in enzymatic digests is critical for confident protein identification and characterization in proteomics research. Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR-MS) can provide low or sub-ppm mass accuracy and ultrahigh resolving power. While for ESI-FT-ICR-MS, the mass accuracy is generally 1 ppm or better, with matrix-assisted laser desorption/ionization (MALDI)-FT-ICR-MS, the mass errors can vary from sub-ppm with internal calibration to over 100 ppm with conventional external calibration. A novel calibration method for N-15-metabolically labeled peptides from a batch digest of a proteome is described which corrects for space charge induced frequency shifts in FT-ICR spectra without using an internal calibrant. This strategy utilizes the information from the mass difference between the N-14/N-15 peptide peak pairs to correct for space charge induced mass shifts after data collection. A procedure for performing the mass correction has been written into a computer program and has been successfully applied to high-performance liquid chromatography-MALDI-FT-ICR-MS measurement of N-15-metabolic labeled proteomes. We have achieved an average measured mass error of 1.0 ppm and a standard deviation of 3.5 ppm for 900 peptides from 68 MALDI-FT-ICR mass spectra of the proteolytic digest of a proteome from Methanococcus maripaludis.
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