Original paper

Peptide identifications and false discovery rates using different mass spectrometry platforms

Volume: 182, Pages: 456 - 463
Published: May 1, 2018
Abstract
Characterization of endogenous neuropeptides produced from post-translational proteolytic processing of precursor proteins is a demanding task. A variety of complex prohormone processing steps generate molecular diversity from neuropeptide prohormones, making in silico neuropeptide discovery difficult. In addition, the wide range of endogenous peptide concentrations as well as significant peptide complexity further challenge the structural...
Paper Details
Title
Peptide identifications and false discovery rates using different mass spectrometry platforms
Published Date
May 1, 2018
Journal
Volume
182
Pages
456 - 463
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