Mass spectrometric measurements were carried out according to the procedure described in a previous study [43 (link)]. The analysis was performed using a Q Exactive HF mass spectrometer (HF Hybrid Quadrupole Orbitrap mass spectrometer, Thermo Fisher Scientific™, Rockwell, IL, USA). Mass spectra were obtained with a resolution of 60,000 (MS) and 15,000 (MS/MS) in the m/z range 400–1500 (MS) and 200–2000 (MS/MS).
The resulting RAW files, unprocessed with a mass spectrometer, were analyzed with the maxquant program (version 1.5.5.1, Jurgen Cox, Max Planck Institute for Biochemistry, Martinsried, Germany) [44 (link)] with the built-in Andromeda search system [45 (link)].
Protein N-terminal acetylation and methionine oxidation were variable modifications for the peptide search. A maximum mass deviation of 5 ppm was allowed for precursor identification, and 20 ppm was set as a tolerance for fragment identification. For trypsin digestion, 2 missing sites were allowed. The false discovery rate (FDR) of resulting protein identifications was 0.01.
The resulting RAW files, unprocessed with a mass spectrometer, were analyzed with the maxquant program (version 1.5.5.1, Jurgen Cox, Max Planck Institute for Biochemistry, Martinsried, Germany) [44 (link)] with the built-in Andromeda search system [45 (link)].
Protein N-terminal acetylation and methionine oxidation were variable modifications for the peptide search. A maximum mass deviation of 5 ppm was allowed for precursor identification, and 20 ppm was set as a tolerance for fragment identification. For trypsin digestion, 2 missing sites were allowed. The false discovery rate (FDR) of resulting protein identifications was 0.01.
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