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Applying mass spectrometry to study non-covalent biomolecule complexes.
Journal article

Applying mass spectrometry to study non-covalent biomolecule complexes.

  • Chen F Department of Chemistry and Applied Biosciences, ETH Zürich, CH-8093, Zürich, Switzerland.
  • Gülbakan B Institute of Child Health, Division of Pediatric Basic Sciences, Hacettepe University, 06100 Ankara, Turkey.
  • Weidmann S Department of Chemistry and Applied Biosciences, ETH Zürich, CH-8093, Zürich, Switzerland.
  • Fagerer SR Department of Chemistry and Applied Biosciences, ETH Zürich, CH-8093, Zürich, Switzerland.
  • Ibáñez AJ Department of Chemistry and Applied Biosciences, ETH Zürich, CH-8093, Zürich, Switzerland.
  • Zenobi R Department of Chemistry and Applied Biosciences, ETH Zürich, CH-8093, Zürich, Switzerland.
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  • 2015-05-07
Published in:
  • Mass spectrometry reviews. - 2016
ESI
MALDI
chemical cross-linking
first shot phenomenon
non-covalent interactions
Biochemistry
Biophysics
Cross-Linking Reagents
Crystallography, X-Ray
Glutaral
Mass Spectrometry
Multiprotein Complexes
Spectrometry, Mass, Electrospray Ionization
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
English Non-covalent interactions are essential for the structural organization of biomacromolecules and play an important role in molecular recognition processes, such as the interactions between proteins, glycans, lipids, DNA, and RNA. Mass spectrometry (MS) is a powerful tool for studying of non-covalent interactions, due to the low sample consumption, high sensitivity, and label-free nature. Nowadays, native-ESI MS is heavily used in studies of non-covalent interactions and to understand the architecture of biomolecular complexes. However, MALDI-MS is also becoming increasingly useful. It is challenging to detect the intact complex without fragmentation when analyzing non-covalent interactions with MALDI-MS. There are two methodological approaches to do so. In the first approach, different experimental and instrumental parameters are fine-tuned in order to find conditions under which the complex is stable, such as applying non-acidic matrices and collecting first-shot spectra. In the second approach, the interacting species are "artificially" stabilized by chemical crosslinking. Both approaches are capable of studying non-covalently bound biomolecules even in quite challenging systems, such as membrane protein complexes. Herein, we review and compare native-ESI and MALDI MS for the study of non-covalent interactions.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/295401
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