Many different approaches for protein quantification have been published in the past few years. Some of them are applied directly to raw data (e.g. SuperHirn (), MaxQuant (), Progenesis (), and OpenMS ()), primarily to obtain quantitative information in the form of intensities or spectral counts for the peptides. Other tools are exclusively designed to combine or transform peptide abundances into quantitative data at the protein level (e.g. emPAI (), APEX (), mSCI (), TOPn (), MSstats (), SIN (), and SRMstats ()). Further differences between the approaches arise from their use of peak intensities or spectral counts as measures for the peptide abundance, whether they specialize in absolute or relative quantification, which mass spectrometric technique is used (discovery-driven, directed or targeted MS ()) and which, if any, isotopic labeling of the peptides is supported. Most publications proposing a procedure based on peptide intensities actually provide an elaborate solution for quantifying peptides (allowing one to combine replicates or normalize the data) but rely on a very simple averaging approach to combine these scores into estimates for protein concentrations. Notably, none of the methods mentioned above—including methods based on spectral counts—take full advantage of the information withheld in shared peptides. Instead, the degenerate peptides are grouped, reassigned to single proteins, or even discarded in order to derive a simple solution to the identification and quantification of proteins. Studies focusing on the inclusion of shared peptides in the protein quantification process include Refs. –., For instance, one would like to be able to identify which are the most or least abundant proteins in a sample, or to compare the concentration of the same protein in two samples taken under different biological conditions., My goal is to detect the important proteins which are connected to the bait protein through creating protein-protein interaction network. I'd like to compare trtA-Exp1 and trtA-Exp2.