Ltq obitrap etd mass spectrometry

The peptide samples were analyzed on Thermo Fisher LTQ Obitrap ETD mass spectrometry, briefly, loaded sample onto an HPLC chromatography system named Thermo Fisher Easy‐nLC 1000 equipped with a C18 column (1.8 mm, 0.15 × 1,00 mm). Solvent A contained 0.1% formic acid and solvent B contained 100% acetonitrile. The elution gradient was from 4% to 18% in 182 min, 18% to 90% in 13 min solvent B at a flow rate of 300 nL/min. Mass spectrometry analysis were carried out carried out at the AIMSMASS Co., Ltd. (Shanghai, China) in the positive‐ion mode with an automated data‐dependent MS/MS analysis with full scans (350‐1600 m/z) acquired using FTMS at a mass resolution of 30,000 and the 10 most intense precursor ions were selected for MS/MS. The MS/MS was acquired using higher‐energy collision dissociation at 35% collision energy at a mass resolution of 15,000.

The peptide samples were analyzed on Thermo Fisher LTQ Obitrap ETD mass spectrometry, Briefly, loaded sample onto an HPLC chromatography system named Thermo Fisher Easy-nLC 1000 equipped with a C18 colume (1.8 mm, 0.15 × 1.00 mm). Solvent A contained 0.1% formic acid and solvent B contained 100% acetonitrile. The elution gradient was from 4 to 18% in 182 min, 18 to 90% in 13 min solvent B at a flow rate of 300 nl/min. Mass spectrometry analysis were carried out carried out at the AIMS Scientific Co.,Ltd.(Shanghai, China) in the positive-ion mode with an automated data-dependent MS/MS analysis with full scans (350–1600 m/z) acquired using FTMS at a mass resolution of 30,000 and the ten most intense precursor ions were selected for MS/MS. The MS/MS was acquired using higher-energy collision dissociation at 35% collision energy at a mass resolution of 15,000.