High pressure MALDI-FTMS: implications for proteomics

Tandem mass spectra of multiply charged ions typically generate more complete fragmentation patterns and thus are desirable for peptide sequencing. However, multiply charged species are not typically observed in spectra obtained with matrix-assisted laser desorption/ionization (MALDI) Fourier transform mass spectrometers. Current efforts with high pressure (HP) MALDI-Fourier transform mass spectrometry (FTMS) have resulted in abundant production of multiply charged ions, introducing the potential for new investigations into the MALDI ion formation mechanism, and increasing the utility of tandem mass spectrometry with MALDI-FTMS. This work focuses on the use of an HP MALDI-FTMS instrument for proteomics applications. The performance of HP MALDI and the power of FTMS and MS/MS of multiply charged ions for proteomics applications are discussed. (C) 2004 Elsevier B.V. All rights reserved.