| Autor: |
Zhao H; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK., Creese AJ; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK., Cooper HJ; School of Biosciences, University of Birmingham, Edgbaston, Birmingham, B15 2TT, UK. h.j.cooper@bham.ac.uk. |
| Abstrakt: |
High-field asymmetric waveform ion mobility spectrometry (FAIMS) is a gas-phase separation technique which, when coupled with liquid chromatography tandem mass spectrometry, offers benefits for analysis of complex proteomics samples such as those encountered in phosphoproteomics experiments. Results from LC-FAIMS-MS/MS are typically complementary, in terms of proteome coverage and isomer identification, to those obtained by use of solution-phase separation methods, such as prefractionation with strong cation-exchange chromatography. Here, we describe the protocol for large-scale phosphorylation analysis by LC-FAIMS-MS/MS. |
