Journal
MASS SPECTROMETRY REVIEWS
Volume 27, Issue 1, Pages 1-19Publisher
JOHN WILEY & SONS INC
DOI: 10.1002/mas.20152
Keywords
MALDI; data analysis; peptides; proteins; nucleic acids
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Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been successfully applied to elucidating biological questions trough the analysis of proteins, peptides, and nucleic acids. Here, we review the different approaches for analyzing the data that is generated by MALDI-MS. The first step in the analysis is the processing of the raw data to find peaks that correspond to the analytes. The peaks are characterized by their areas (or heights) and their centroids. The peak area can be used as a measure of the quantity of the analyte, and the centroid can be used to determine the mass of the analyte. The masses are then compared to models of the analyte, and these models are ranked according to how well they fit the data and their significance is calculated. This allows the determination of the identity (sequence and modifications) of the analytes. We show how this general data analysis workflow is applied to protein and nucleic acid chemistry as well as proteomics. (c) 2007 Wiley Periodicals, Inc.
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