%0 Journal Article %T Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry. %+ Imagerie Moléculaire et Nanobiotechnologies - Institut Européen de Chimie et Biologie (IECB) %+ Laboratoire de Biochimie de l'Ecole polytechnique (BIOC) %+ Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) %+ Laboratoire de Physico -& Toxico Chimie des systèmes naturels (LPTC) %A Belghazi, M. %A Bathany, K. %A Hountondji, Codjo %A Grandier-Vazeille, X. %A Manon, S. %A Schmitter, J.-M. %< avec comité de lecture %@ 1615-9853 %J Proteomics %I Wiley-VCH Verlag %V 1 %N 8 %P 946-54 %8 2001-08 %D 2001 %R 10.1002/1615-9861(200108)1:8<946::AID-PROT946>3.0.CO;2-P %M 11683511 %Z Life Sciences [q-bio]/Biochemistry, Molecular BiologyJournal articles %X In the context of proteome analysis, matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) can fulfil the two tasks of primary structure verification and protein identification. As an illustration of the first of these tasks, the sequence of Eschericha coli isoleucyl-tRNA synthetase, a protein with 15 reported sequence conflicts, has been established by means of MALDI mass mapping. The identification of mitochondrial proteins participating in a yeast supramolecular complex exhibiting NADH dehydrogenase activity highlights the performances of MALDI-MS for the second task. The spectral suppression phenomenon occurring for complex peptide mixtures analysed by MALDI is discussed, as well as the role of post-source decay analysis for confident protein identification. %G English %L hal-00771534 %U https://polytechnique.hal.science/hal-00771534 %~ X %~ CNRS %~ IGBMC %~ UNIV-STRASBG %~ X-BIOCH %~ X-DEP %~ X-DEP-BIO %~ SITE-ALSACE