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- Title
APPLYING MASS SPECTROMETRY TO STUDY NON-COVALENT BIOMOLECULE COMPLEXES.
- Authors
Chen, Fan; Gülbakan, Basri; Weidmann, Simon; Fagerer, Stephan R.; Ibáñez, Alfredo J.; Zenobi, Renato
- Abstract
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 noncovalent 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 tofind 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 noncovalently 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.
- Subjects
BIOMOLECULES spectra; MASS spectrometry; CROSSLINKING (Polymerization); GLYCAN structure; NUCLEIC acids spectra; RNA
- Publication
Mass Spectrometry Reviews, 2016, Vol 35, Issue 1, p48
- ISSN
0277-7037
- Publication type
Article
- DOI
10.1002/mas.21462