Evaluation of TIMS-derived peptide mobility measurements: calibration strategy and MS1/MS2 discrepancies

The widespread adoption of trapped ion mobility coupled to mass spectrometry for proteome analysis necessitates high-quality data measurement of both ion mobility and mass spectra. In this study, the accuracy of ion mobility measurements in the context of mass spectral (MS) library building and searching is evaluated. Key factors influencing measurement accuracy, such as calibration strategy and the timing of acquisition relative to the chromatographic apex, are systematically investigated. A calibration system based on a synthetic peptide mixture is shown to improve calibration performance. Further, reproducibility of MS1- and MS2-associated mobility measurements in data-dependent acquisition (DDA) is analyzed. Overall, this work identifies methods to improve ion mobility measurement accuracy for proteomics analyses using a standardized synthetic peptide mixture.

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Publication Details

Journal
Analytical and Bioanalytical Chemistry
Published
2026-06-26
DOI
https://doi.org/10.1007/s00216-026-06633-9
Primary Topic
Advanced Proteomics Techniques and Applications
Type
article
Field-Weighted Citation Impact
0.00

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article

Evaluation of TIMS-derived peptide mobility measurements: calibration strategy and MS1/MS2 discrepancies

Anh Q. Tran, Tytus Mak, Meghan Burke Harris
Analytical and Bioanalytical Chemistry
Advanced Proteomics Techniques and Applications
article

Evaluation of TIMS-derived peptide mobility measurements: calibration strategy and MS1/MS2 discrepancies

Anh Q. Tran, Tytus Mak, Meghan Burke Harris
article en

Abstract

The widespread adoption of trapped ion mobility coupled to mass spectrometry for proteome analysis necessitates high-quality data measurement of both ion mobility and mass spectra. In this study, the accuracy of ion mobility measurements in the context of mass spectral (MS) library building and searching is evaluated. Key factors influencing measurement accuracy, such as calibration strategy and the timing of acquisition relative to the chromatographic apex, are systematically investigated. A calibration system based on a synthetic peptide mixture is shown to improve calibration performance. Further, reproducibility of MS1- and MS2-associated mobility measurements in data-dependent acquisition (DDA) is analyzed. Overall, this work identifies methods to improve ion mobility measurement accuracy for proteomics analyses using a standardized synthetic peptide mixture.

Analytical and Bioanalytical Chemistry
Physical Measurement Laboratory (US), Material Measurement Laboratory (US)
National Institute of Standards and Technology
Openalex Percentile: Top 13%
Advanced Proteomics Techniques and Applications
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