John H. Robinson

TL;DR: The proteome of normal male urine from a commercial pooled source has been examined using direct liquid chromatography‐tandem mass spectrometry (LC‐MS/MS), and the experimental time for these analyses was less than that required to run a single two‐dimensional gel.

TL;DR: Off-line validation of the platform showed near quantitative recovery of fractionated peptides and essentially complete ion-exchange partitioning, and in comparative analyses of a highly complex peptide digest mixture a >40% increase in the number of peptide and protein identifications was achieved.

TL;DR: Operational and post‐analysis strategies are presented to restore data confidence and reconcile the greatest number of matched spectra and the impact on data fidelity as a product of data‐dependent selection of precursor ions from a dynamically excluded field is discussed.

TL;DR: An affinity selection method to capture cysteinyl peptides and thereby simplify the mixture and was applied to the analysis of a protein fraction obtained from isolated mitochondria treated with atractyloside.

TL;DR: Improved tandem mass spectrometry (MS/MS) spectra were generated, facilitating identification of proteins at a low pmol level, and application of this technology to the identification of a standard protein and an unknown from an affinity‐enriched mixture are shown.