Lyutvinskiy, YaroslavNagornov, Konstantin O.Kozhinov, Anton N.Gasilova, NataliaMenin, LaureMeng, ZhaoweiZhang, XuepeiSaei, Amir AtaFu, TingtingChamot-Rooke, JuliaTsybin, Yury O.Makarov, AlexanderZubarev, Roman A.2024-05-012024-05-012024-05-012024-04-1210.1021/jasms.3c00442https://infoscience.epfl.ch/handle/20.500.14299/207705WOS:001203928900001Traditionally, mass spectrometry (MS) output is the ion abundance plotted versus the ionic mass-to-charge ratio m/z. While employing only commercially available equipment, Charge Determination Analysis (CHARDA) adds a third dimension to MS, estimating for individual peaks their charge states z starting from z = 1 and color coding z in m/z spectra. CHARDA combines the analysis of ion signal decay rates in the time-domain data (transients) in Fourier transform (FT) MS with the interrogation of mass defects (fractional mass) of biopolymers. Being applied to individual isotopic peaks in a complex protein tandem (MS/MS) data set, CHARDA aids peptide mass spectra interpretation by facilitating charge-state deconvolution of large ionic species in crowded regions, estimating z even in the absence of an isotopic distribution (e.g., for monoisotopic mass spectra). CHARDA is fast, robust, and consistent with conventional FTMS and FTMS/MS data acquisition procedures. An effective charge-state resolution R-z >= 6 is obtained with the potential for further improvements.Life Sciences & BiomedicinePhysical SciencesTechnologyMass SpectrometryPolypeptideProteomicsSpectrumtext::journal::journal article::research article