A graph-based approach for proteoform identification and quantification using top-down homogeneous multiplexed tandem mass spectra.
BACKGROUND
Top-down homogeneous multiplexed tandem mass (HomMTM) spectra are generated from modified proteoforms of the 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 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.
['Zhu|Kaiyuan|K|', 'Liu|Xiaowen|X|']
D000465:Algorithms D002853:Chromatography, Liquid D006657:Histones D006801:Humans D008970:Molecular Weight D011499:Protein Processing, Post-Translational D020543:Proteome D040901:Proteomics D053719:Tandem Mass Spectrometry
Top-down Mass spectrometry Graph algorithms Multiplexed mass spectra