Natural isotope correction improves analysis of protein modification dynamics

        Stable isotope labelling in combination with high-resolution mass spectrometry approaches are increasingly used to analyze both metabolite and protein modification dynamics. To enable correct estimation of the resulting dynamics, it is critical to correct the measured values for naturally occurring stable isotopes, a process commonly called isotopologue correction or deconvolution. While the importance of isotopologue correction is well recognized in metabolomics, it has received far less attention in proteomics approaches. Although several tools exist that enable isotopologue correction of mass spectrometry data, the majority is tailored for the analysis of low molecular weight metabolites. We here present PICor which has been developed for isotopologue correction of complex isotope labelling experiments in proteomics or metabolomics and demonstrate the importance of appropriate correction for accurate determination of protein modifications dynamics, using histone acetylation as an example.


DOI: 10.1007/s00216-021-03732-7

Projects: MESI-STRAT

Publication type: Journal

Journal: Analytical and Bioanalytical Chemistry

Citation: Anal Bioanal Chem 413(30):7333-7340

Date Published: 1st Dec 2021

Registered Mode: by DOI

Authors: Jörn Dietze, Alienke van Pijkeren, Anna-Sophia Egger, Mathias Ziegler, Marcel Kwiatkowski, Ines Heiland

help Submitter
Dietze, J., van Pijkeren, A., Egger, A.-S., Ziegler, M., Kwiatkowski, M., & Heiland, I. (2021). Natural isotope correction improves analysis of protein modification dynamics. In Analytical and Bioanalytical Chemistry (Vol. 413, Issue 30, pp. 7333–7340). Springer Science and Business Media LLC.

Views: 822

Created: 11th Jan 2022 at 09:59

Last updated: 8th Dec 2022 at 18:26

help Tags

This item has not yet been tagged.

help Attributions


Powered by
Copyright © 2008 - 2023 The University of Manchester and HITS gGmbH