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Protein sequence information by matrix‐assisted laser desorption/ionization in‐source decay mass spectrometry
Author(s) -
Hardouin Julie
Publication year - 2007
Publication title -
mass spectrometry reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 126
eISSN - 1098-2787
pISSN - 0277-7037
DOI - 10.1002/mas.20142
Subject(s) - chemistry , mass spectrometry , matrix assisted laser desorption/ionization , sequence (biology) , matrix (chemical analysis) , ionization , protein mass spectrometry , desorption , analytical chemistry (journal) , chromatography , surface enhanced laser desorption/ionization , tandem mass spectrometry , ion , biochemistry , organic chemistry , adsorption
Proteins from biological samples are often identified by mass spectrometry (MS) with the two following “bottom‐up” approaches: peptide mass fingerprinting or peptide sequence tag. Nevertheless, these strategies are time‐consuming (digestion, liquid chromatography step, desalting step), the N ‐ (or C ‐) terminal information often lacks and post‐translational modifications (PTMs) are hardly observed. The in‐source decay (ISD) occurring in a matrix assisted laser desorption/ionization (MALDI) source appears an interesting analytical tool to obtain N ‐terminal sequence, to identify proteins and to characterize PTMs by a “top‐down” strategy. The goal of this review deals with the usefulness of the ISD technique in MALDI source in proteomics fields. In the first part, the ISD principle is explained and in the second part, the use of ISD in proteomic studies is discussed for protein identification and sequence characterization. © 2007 Wiley Periodicals, Inc., Mass Spec Rev 26:672–682, 2007