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Intact protein analysis by matrix‐assisted laser desorption/ionization tandem time‐of‐flight mass spectrometry
Author(s) -
Lin Melanie,
Campbell Jennifer M.,
Mueller Dieter R.,
Wirth Urs
Publication year - 2003
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1102
Subject(s) - chemistry , mass spectrometry , tandem mass spectrometry , ion , fragmentation (computing) , top down proteomics , protein mass spectrometry , sample preparation in mass spectrometry , tandem , analytical chemistry (journal) , chromatography , yield (engineering) , time of flight mass spectrometry , surface enhanced laser desorption/ionization , ionization , matrix assisted laser desorption/ionization , desorption , electrospray ionization , organic chemistry , materials science , composite material , operating system , adsorption , computer science , metallurgy
Direct tandem mass spectrometric (MS/MS) analysis of small, singly charged protein ions by tandem time‐of‐flight mass spectrometry (TOFMS) is demonstrated for proteins up to a molecular mass of 12 kDa. The MALDI‐generated singly charged precursor ions predominantly yield product ions resulting from metastable fragmentation at aspartyl and prolyl residues. Additional series of C‐terminal sequence ions provide in some cases sufficient information for protein identification. The amount of sample required to obtain good quality spectra is in the high femtomolar to low picomolar range. Within this range, MALDI‐MS/MS using TOF/TOF™ ion optics now provides the opportunity for direct protein identification and partial characterization without prior enzymatic hydrolysis. Copyright © 2003 John Wiley & Sons, Ltd.