Abstract
We combined high performance liquid chromatography and tandem mass spectrometry (HPLC-MS/MS) with bioinformatics tools to analyze the isobaric modified peptides which were methylated and dimethylated at either lysine (K) 27 or/and K36 from histone H3. They were identified and dissected through alignment of every fragment ion, and the two modified sites were further analyzed according to their relative intensities of MS/MS spectra.
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