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Protein phosphorylation plays a key role in cellular progresses.Selective detection of phosphopeptides from proteolytic digests is a challenging and highly relevant task due to the low abundance of phosphoproteins in complex biological samples.Mass spectrometry (MS), such as MALDI-TOF MS, is a powerful tool to characterize protein phosphorylation because of its high sensitivity.However, direct mass spectrometric ananlysis of phosphopeptides is far from satisfactory because it suffers from the well-known ion suppression effect.