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Rachelle lee timenet1/1/2023 ![]() ![]() Integration of Mass Spectrometry Data for Structural Biology. Britt, Tristan Cragnolini, Konstantinos Thalassinos. This article is cited by 109 publications. The effective peak capacities in analyses of tryptic peptides are ∼500 for FAIMS/IMS separations and ∼10 6 for 3-D FAIMS/IMS/MS, providing a potential platform for ultrahigh-throughput analyses of complex mixtures. ![]() Evaluation of FAIMS/IMS/TOF performance for a protein mixture tryptic digest reveals high orthogonality between FAIMS and IMS dimensions and, hence, the benefit of FAIMS filtering prior to IMS/MS. Implementation of FAIMS/IMS and IMS/MS interfaces using electrodynamic ion funnels greatly improves sensitivity. We report 2-D gas-phase separations that join FAIMS to IMS, in conjunction with high-resolution and accuracy time-of-flight (TOF) MS. However, modest separation peak capacities have limited the utility of FAIMS and IMS for analyses of complex mixtures. A major attraction of these separations is extremely high speed, exceeding that of condensed-phase alternatives by orders of magnitude. ![]() Coupled to mass spectrometry (MS), both IMS and FAIMS have shown the potential for broad utility in proteomics and other biological analyses. Recently, field asymmetric waveform IMS (FAIMS) has been gaining acceptance in similar applications. Ion mobility spectrometry (IMS) has been explored for decades, and its versatility in separation and identification of gas-phase ions is well established. ![]()
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