Natural isotope correction improves analysis of protein modification dynamics

Stable isotope labelling in combination with high resolution mass spectrometry approaches are increasingly used to analyse 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, none of them is universally applicable for all potential experimental approaches. We here present PICor which has been streamlined for multiple isotope labelling isotopologue correction in proteomics or metabolomics approaches. We demonstrate the importance for accurate measurement of the dynamics of protein modifications, such as histone acetylation.

Cверхтонкая структура в ЭПР изотопов -=SUP=-151-=/SUP=-Eu-=SUP=-2+-=/SUP=- и -=SUP=-153-=/SUP=-Eu-=SUP=-2+-=/SUP=- в лютеций-алюминиевом гранате

Electron paramagnetic resonance of rhombic Eu^2+ centers in single crystals of Lu_3Al_5O_12 doped with europium ions with the natural isotope abundance was studied. Parameters of the hyperfine and quadrupole interactions of ^151Eu and ^153Eu isotopes of these centers were determined.