Analysis of protein sequences and protein complexes by matrix-assisted laser desorption/ionization mass spectrometry.
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.
Belghazi
M
M
Institut Européen de Chimie Biologie, Talence, France.
Bathany
K
K
Hountondji
C
C
Grandier-Vazeille
X
X
Manon
S
S
Schmitter
J M
JM
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology; D007533:Isoleucine-tRNA Ligase / Q000737:chemistry*; D008718:Methionine-tRNA Ligase / Q000737:chemistry*; D008928:Mitochondria / Q000201:enzymology; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
D008718:Methionine-tRNA Ligase; D007533:Isoleucine-tRNA Ligase