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Updated: May 24, 2026

Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
Published on: September 9, 2013
MALDI-ToF mass spectrometry for studying noncovalent complexes of biomolecules
Stefanie Mädler1, Elisabetta Boeri Erba, Renato Zenobi
1Department of Chemistry and Applied Biosciences, ETH Zurich, 8093, Zurich, Switzerland.
Abstract:
Matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) has been demonstrated to be a valuable tool to investigate noncovalent interactions of biomolecules. The direct detection of noncovalent assemblies is often more troublesome than with electrospray ionization. Using dedicated sample preparation techniques and carefully optimized instrumental parameters, a number of biomolecule assemblies were successfully analyzed. For complexes dissociating under MALDI conditions, covalent stabilization with chemical cross-linking is a suitable alternative. Indirect methods allow the detection of noncovalent assemblies by monitoring the fading of binding partners or altered H/D exchange patterns.
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