Abstract
Matrix-assisted laser-desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) offers a number of advantages, including the ability to analyze mixtures of peptides, a high sensitivity, a good tolerance for buffers and salts, and also the ability to perform peptide fragmentation analysis. For these reasons, MALDI-TOF MS alone or combined with Post- Source-Decay/Collision-Induced-Dissociation (PSD/CID) has been proven to be a powerful tool for the identification and localization of posttranslational modifications of proteins.
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CITATION STYLE
Redeker, V., Vinh, J., Le Caer, J. P., & Rossier, J. (1998). Characterization of posttranslational modifications of proteins by MALDI-TOF MS: Application to the study of tubulin. Analusis. Societe Francaise de Chimie. https://doi.org/10.1051/analusis:1998260022
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