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Natural isotope correction improves analysis of protein modification dynamics.

Authors :
Dietze J
van Pijkeren A
Egger AS
Ziegler M
Kwiatkowski M
Heiland I
Source :
Analytical and bioanalytical chemistry [Anal Bioanal Chem] 2021 Dec; Vol. 413 (30), pp. 7333-7340. Date of Electronic Publication: 2021 Oct 27.
Publication Year :
2021

Abstract

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.<br /> (© 2021. The Author(s).)

Details

Language :
English
ISSN :
1618-2650
Volume :
413
Issue :
30
Database :
MEDLINE
Journal :
Analytical and bioanalytical chemistry
Publication Type :
Academic Journal
Accession number :
34705077
Full Text :
https://doi.org/10.1007/s00216-021-03732-7