Ion Mobility Mass Spectrometry in Structural Biology
Summary
Ion mobility mass spectrometry (IM-MS) has emerged as a transformative approach in structural biology by integrating gas-phase ion separation based on mobility with high-resolution mass analysis. In a typical IM-MS workflow, biomolecular ions generated by electrospray ionisation are guided through a buffer gas under an electric field, allowing separation according to size, shape and charge before entering a mass analyser. The resulting measurements of mass, charge state and collision cross section (CCS) yield multidimensional data that reveal conformational landscapes, distinguish isomeric or isobaric species and track dynamic processes such as folding, ligand binding and complex assembly. By preserving native-like interactions, IM-MS can probe membrane proteins, multisubunit assemblies and intrinsically disordered proteins in ways that complement crystallography, cryo-EM and NMR. Advances in coupling mobility separation with collision- or photon-induced activation, as well as the integration of computational modelling, have further enhanced confidence in structural assignments and enabled studies of transient states. Continuous innovation in instrument design, data-processing algorithms and standardisation of reporting practices is extending the reach of IM-MS from single complexes to proteome-scale analyses and challenging targets such as viral capsids and dynamic protein networks.
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Ion Mobility Mass Spectrometry in Structural Biology publication trend
The graph below shows the total number of articles in ion mobility mass spectrometry in structural biology across all publications each year (not limited to Nature Index journals).
Technical terms
Ion mobility mass spectrometry (IM-MS): A technique combining gas-phase ion separation by mobility with mass analysis to measure size, shape and mass of biomolecular ions.
Collision cross section (CCS): A parameter derived from ion mobility measurements that reflects the effective gas-phase surface area of an ion, related to its conformation.
Drift tube ion mobility spectrometry (DTIMS): A form of IM-MS in which ions travel through a uniform electric field and collide with buffer gas molecules, separating by mobility.
Travelling wave ion mobility spectrometry (TWIMS): A mobility separation method using a sequence of voltage pulses to propel ions through a gas-filled cell, enabling compact instrument designs.
Intrinsically disordered protein (IDP): A protein or region lacking a fixed tertiary structure under physiological conditions, often characterised by dynamic conformational ensembles.
References
- Ion Mobility Mass Spectrometry (IM-MS) for Structural Biology: Insights Gained by Measuring Mass, Charge, and Collision Cross Section. Chemical Reviews (2023).
- Recommendations for reporting ion mobility Mass Spectrometry measurements. Mass Spectrometry Reviews (2019).
- Ion mobility mass spectrometry of peptide, protein, and protein complex ions using a radio-frequency confining drift cell. Analyst (2016).
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