Identification of Two Novel Modifications at Tryptophan Residues.
Protein post-translational modifications (PTMs) play important roles in cellular physiology. Mass spectrometry (MS) has been developed into a powerful tool to identify all possible protein modifications. Herein, we describe our efforts to deduce the structures of two unknown modifications at tryptophan (Trp) residues (W + 92 Da and W + 108 Da). The two modifications were further confirmed by aligning the MS/MS fragmentation of synthetic peptide with in-vivo peptide identified. Finally, the mimic experiment elucidated how two Trp modifications occur. This study, therefore, expands current knowledge of Trp modifications.
['Zheng|Shuzhen|S|', 'Zhang|Kai|K|', 'Tian|Shanshan|S|', 'He|Xiwen|X|', 'Zhang|Yukui|Y|']
D011499:Protein Processing, Post-Translational D040901:Proteomics D053719:Tandem Mass Spectrometry D014364:Tryptophan
Post-translational modifications Mass spectrometry Proteomics Tryptophan modifications