Ion mobility-mass spectrometry of supramolecular complexes and assemblies
Kalenius, E., Groessl, M., & Rissanen, K. (2019). Ion mobility-mass spectrometry of supramolecular complexes and assemblies. Nature Reviews Chemistry, 3(1), 4-14. https://doi.org/10.1038/s41570-018-0062-2
Published inNature Reviews Chemistry
© Macmillan Publishers Limited, part of Springer Nature, 2019.
Despite their structural and functional differences, synthetic supramolecular assemblies share many similarities with biological assemblies, especially enzymes. The assemblies can be on the same length scale, and their structures and guest binding are typically governed by non-covalent interactions. Thus, only relatively weak interactions define the shape of a synthetic supramolecule or the secondary and tertiary structure of a protein, such that the resulting dynamism makes structure elucidation challenging. For biomolecules such as peptides, proteins, glycans and lipids this has often been tackled using ion mobility–mass spectrometry (IM-MS), whereby analyte ions are separated according to their gas-phase mobility and their mass-to-charge ratio. IM-MS is an established method in omics, separation sciences and small-molecule structural chemistry, but has only recently grown in popularity for the study of synthetic supramolecular assemblies in the gas phase. This Review describes IM-MS techniques and how they can help us understand the structures of molecular self-assemblies, host–guest complexes and metallosupramolecular complexes. ...
PublisherNature Publishing Group
Publication in research information system
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Related funder(s)Academy of Finland
Funding program(s)Research costs of Academy Research Fellow, AoF
Additional information about fundingThe authors thank the Academy of Finland (project numbers 284562 and 312514) and the University of Jyväskylä for financial support.
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