Peptide identifications and false discovery rates using different mass spectrometry platforms.

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 characterization of neuropeptides. Liquid chromatography-mass spectrometry (MS), performed in conjunction with bioinformatics, allows for high-throughput characterization of peptides. Mass analyzers and molecular dissociation techniques render specific characteristics to the acquired data and thus, influence the analysis of the MS data using bioinformati

SUBMITTER: Anapindi KDB 

PROVIDER: S-EPMC5839655 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature