Abstract Background Top-down homogeneous multiplexed tandem mass (HomMTM) spectra are generated from modified proteoforms of the sara stedy stand aid same protein with different post-translational modification patterns.They are frequently observed in the analysis of ultramodified proteins, some proteoforms of which have similar molecular weights and cannot be well separated by liquid chromatography in mass spectrometry analysis.Results We formulate the top-down HomMTM spectral identification problem as the minimum error read more k-splittable flow problem on graphs and propose a graph-based algorithm for the identification and quantification of proteoforms using top-down HomMTM spectra.
Conclusions Experiments on a top-down mass spectrometry data set of the histone H4 protein showed that the proposed method identified many proteoform pairs that better explain the query spectra than single proteoforms.