@article{
 title = {Absorption-mode fourier transform mass spectrometry: The effects of apodization and phasing on modified protein spectra},
 type = {article},
 year = {2013},
 keywords = {Absorption-mode,Apodization,Harmonics,Top-down},
 volume = {24},
 id = {8c148be9-2105-3c5d-a367-d977676ddcc1},
 created = {2019-02-14T18:15:56.236Z},
 file_attached = {false},
 profile_id = {9f6c4084-7a51-3e30-8518-5a3d275e6797},
 last_modified = {2019-02-14T18:15:56.236Z},
 read = {false},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {The method of phasing broadband Fourier transform ion cyclotron resonance (FT-ICR) spectra allows plotting the spectra in the absorption-mode; this new approach significantly improves the quality of the data at no extra cost. Herein, an internal calibration method for calculating the phase function has been developed and successfully applied to the top-down spectra of modified proteins, where the peak intensities vary by 100×. The result shows that the use of absorption-mode spectra allows more peaks to be discerned within the recorded data, and this can reveal much greater information about the protein and modifications under investigation. In addition, noise and harmonic peaks can be assigned immediately in the absorption-mode. [Figure not available: see fulltext.] © 2013 American Society for Mass Spectrometry.},
 bibtype = {article},
 author = {Qi, Y. and Li, H. and Wills, R.H. and Perez-Hurtado, P. and Yu, X. and Kilgour, D.P.A. and Barrow, M.P. and Lin, C. and O'Connor, P.B.},
 doi = {10.1007/s13361-013-0600-6},
 journal = {Journal of the American Society for Mass Spectrometry},
 number = {6}
}

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