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gas_phase_stability_of_protein_ions_in_a_cyclic.pdf (4.67 MB)

Gas Phase Stability of Protein Ions in a Cyclic Ion Mobility Spectrometry Travelling Wave Device

submitted on 27.11.2018 and posted on 28.11.2018 by Charles Eldrid, Jakub Ujma, Symeon Kalfas, nick tomczyk, Kevin Giles, mike morris, Konstantinos Thalassinos
Ion mobility mass spectrometry (IM-MS) allows separation of native protein ions into “conformational families”. Increasing the IM resolving power should allow finer structural information to be obtained, and can be achieved by increasing the length of the IM separator. This, however, increases the time that protein ions spend in the gas phase and previous experiments have shown that the initial conformations of small proteins can be lost within tens of milliseconds. Here, we report on investigations of protein ion stability using a multi-pass travelling wave (TW) cyclic IM (cIM) device. Using this device, minimal structural changes were observed for Cytochrome C after hundreds of milliseconds, while no changes were observed for a larger multimeric complex (Concanavalin A). The geometry of the instrument (Q-cIM-ToF) also enables complex tandem IM experiments to be performed which were used to obtain more detailed collision induced unfolding pathways for Cytochrome C. The novel instrument geometry provide unique capabilities with the potential to expand the field of protein analysis via IM-MS.


Email Address of Submitting Author


University College London


United Kingdom

ORCID For Submitting Author


Declaration of Conflict of Interest

Jakub Ujma, Nick Tomczyk, Kevin Giles and Mike Morris are all employees of Waters Corporation.

Version Notes

Updated collaborator names