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- W4229002009 abstract "Ion mobility spectrometry/mass spectrometry (IMS/MS) is widely used to study various levels of protein structure. Here, we review the current state of affairs in tandem-trapped ion mobility spectrometry/mass spectrometry (tTIMS/MS). Two different tTIMS/MS instruments are discussed in detail: the first tTIMS/MS instrument, constructed from coaxially aligning two TIMS devices; and an orthogonal tTIMS/MS configuration that comprises an ion trap for irradiation of ions with UV photons. We discuss the various workflows the two tTIMS/MS setups offer and how these can be used to study primary, tertiary, and quaternary structures of protein systems. We also discuss, from a more fundamental perspective, the processes that lead to denaturation of protein systems in tTIMS/MS and how to soften the measurement so that biologically meaningful structures can be characterised with tTIMS/MS. We emphasize the concepts underlying tTIMS/MS to underscore the opportunities tandem-ion mobility spectrometry methods offer for investigating heterogeneous samples." @default.
- W4229002009 created "2022-05-08" @default.
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- W4229002009 creator A5034080799 @default.
- W4229002009 creator A5050206948 @default.
- W4229002009 date "2022-01-01" @default.
- W4229002009 modified "2023-10-12" @default.
- W4229002009 title "Tandem-trapped ion mobility spectrometry/mass spectrometry (<i>t</i>TIMS/MS): a promising analytical method for investigating heterogenous samples" @default.
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