Gas phase stability of protein ions in a cyclic ion mobility spectrometry traveling wave device
Gas phase stability of protein ions in a cyclic ion mobility spectrometry traveling wave device
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 multipass traveling 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 instrument geometry provides unique capabilities with the potential to expand the field of protein analysis via IM-MS.
Eldrid, Charles
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Ujma, Jakub
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Kalfas, Symeon
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Tomczyk, Nick
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Giles, Kevin
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Morris, Mike
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Thalassinos, Konstantinos
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18 June 2019
Eldrid, Charles
caf78c85-1eae-4700-814a-01b5f0635a0b
Ujma, Jakub
9c1bc87a-5d3b-443b-bbba-6f52e0dfc327
Kalfas, Symeon
c8f8a25a-825f-4b54-948e-851e93b9997b
Tomczyk, Nick
cfce4cce-9b25-49c0-9dee-fac5bb5f1802
Giles, Kevin
d6e9a32b-4c38-4c6f-8145-2d85383f5fdb
Morris, Mike
90bc2dff-bf7c-460e-9ece-fdc058a0a4a5
Thalassinos, Konstantinos
75b3f786-6a27-420a-8727-97eafb34c022
Eldrid, Charles, Ujma, Jakub, Kalfas, Symeon, Tomczyk, Nick, Giles, Kevin, Morris, Mike and Thalassinos, Konstantinos
(2019)
Gas phase stability of protein ions in a cyclic ion mobility spectrometry traveling wave device.
Analytical Chemistry, 91 (12).
(doi:10.1021/acs.analchem.8b05641).
Abstract
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 multipass traveling 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 instrument geometry provides unique capabilities with the potential to expand the field of protein analysis via IM-MS.
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e-pub ahead of print date: 22 May 2019
Published date: 18 June 2019
Identifiers
Local EPrints ID: 446816
URI: http://eprints.soton.ac.uk/id/eprint/446816
ISSN: 0003-2700
PURE UUID: 13ce86fc-2904-4451-b767-9d813e5633ad
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Date deposited: 23 Feb 2021 17:32
Last modified: 16 Mar 2024 10:53
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Author:
Jakub Ujma
Author:
Symeon Kalfas
Author:
Nick Tomczyk
Author:
Kevin Giles
Author:
Mike Morris
Author:
Konstantinos Thalassinos
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