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Published on: January 20, 2022
Trapped Ion Mobility Spectrometry and Parallel Accumulation-Serial Fragmentation in Proteomics
Florian Meier1, Melvin A Park2, Matthias Mann3
1Department Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, Germany; Functional Proteomics, Jena University Hospital, Jena, Germany.
Trapped ion mobility spectrometry (TIMS) coupled with parallel accumulation-serial fragmentation (PASEF) enhances proteome profiling speed and sensitivity. This advanced technique improves data acquisition and peptide identification for clinical proteomics and single-cell analyses.
Area of Science:
- Analytical Chemistry
- Biochemistry
- Mass Spectrometry
Background:
- Ion mobility spectrometry (IMS) separates ions by size and shape, offering hybridization with LC-MS.
- Recent advancements have renewed interest in IMS due to improved efficiency and implementation.
Purpose of the Study:
- To review developments in trapped ion mobility spectrometry (TIMS) coupled with TOF mass analysis.
- To highlight the advantages of the parallel accumulation-serial fragmentation (PASEF) mode for proteomics.
Main Methods:
- Review of recent literature on TIMS-TOF MS.
- Focus on the PASEF operation mode and its synchronization of ion release and fragmentation.
- Utilizing the correlation between ion mobility and mass for data acquisition.
Main Results:
- PASEF significantly increases the number of peptide fragment ion spectra, enhancing sequencing speed and sensitivity.
- Improved efficiency in both data-dependent and data-independent acquisition methods.
- Enables precise collisional cross-section measurements and prediction using neural networks.
Conclusions:
- TIMS-TOF with PASEF is a powerful platform for rapid proteome profiling and ultrasensitive measurements.
- The technology facilitates accurate peptide identification and characterization of post-translational modifications.
- PASEF expands capabilities for clinical proteomics, single-cell analysis, and beyond.
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