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• W4387002885 abstract "Ion mobility spectrometry-mass spectrometry (IMS-MS) is experiencing rapid growth in proteomic studies, driven by its enhancements in dynamic range and throughput, increasing the quantitation precision, and the depth of proteome coverage. The core principle of ion mobility spectrometry is to separate ions in an inert gas under the influence of an electric field based on differences in drift time. This minireview provides an introduction to IMS operation modes and a description of advantages and limitations is presented. Moreover, the principles of trapped IMS-MS (TIMS-MS), including parallel accumulation-serial fragmentation are discussed. Finally, emerging applications linked to TIMS focusing on sample throughput (in clinical proteomics) and sensitivity (single-cell proteomics) are reviewed, and the possibilities of intact protein analysis are discussed." @default.
• W4387002885 created "2023-09-26" @default.
• W4387002885 creator A5026327822 @default.
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• W4387002885 date "2023-09-01" @default.
• W4387002885 modified "2023-10-06" @default.
• W4387002885 title "Exploiting ion‐mobility mass spectrometry for unraveling proteome complexity" @default.
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• W4387002885 doi "https://doi.org/10.1002/jssc.202300512" @default.
• W4387002885 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37746674" @default.
• W4387002885 hasPublicationYear "2023" @default.
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