title: MALDI-ToF mass spectrometry for studying noncovalent complexes of biomolecules.
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.
authors.affiliation: Department of Chemistry and Applied Biosciences, ETH Zurich, 8093, Zurich, Switzerland.
authors.forename: Stefanie
authors.initials: S
authors.lastname: Mädler
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Boeri Erba
authors.forename: Renato
authors.initials: R
authors.lastname: Zenobi
mesh_terms: D000818:Animals; D003432:Cross-Linking Reagents / Q000737:chemistry; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D041961:Deuterium Exchange Measurement / Q000379:methods; D006801:Humans; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D003432:Cross-Linking Reagents; D011506:Proteins; D004247:DNA