Characterization of peptide-protein relationships in protein ambiguity groups via bipartite graphs
Karin SchorkiD, Michael TurewicziD, Julian UszkoreitiD, Jörg RahnenführeriD, Martin EisenacheriD
Abstract
In bottom-up proteomics, proteins are enzymatically digested into peptides before measurement with mass spectrometry. The relationship between proteins and their corresponding peptides can be represented by bipartite graphs. We conduct a comprehensive analysis of bipartite graphs using quantified peptides from measured data sets as well as theoretical peptides from an in silico digestion of the corresponding complete taxonomic protein sequence databases. The aim of this study is to characterize and structure the different types of graphs that occur and to compare them between data sets. We observed a large influence of the accepted minimum peptide length during in silico digestion. When changing from theoretical peptides to measured ones, the graph structures are subject to two opposite effects. On the one hand, the graphs based on measured peptides are on average smaller and less complex compared to graphs using theoretical peptides. On the other hand, the proportion of protein nodes without unique peptides, which are a complicated case for protein inference and quantification, is considerably larger for measured data. Additionally, the proportion of graphs containing at least one protein node without unique peptides rises when going from database to quantitative level. The fraction of shared peptides and proteins without unique peptides as well as the complexity and size of the graphs highly depends on the data set and organism. Large differences between the structures of bipartite peptide-protein graphs have been observed between database and quantitative level as well as between analyzed species. In the analyzed measured data sets, the proportion of protein nodes without unique peptides ranged from 6.4% to 55.0%. This highlights the need for novel methods that can quantify proteins without unique peptides. The knowledge about the structure of the bipartite peptide-protein graphs gained in this study will be useful for the development of such algorithms.
02 /Specification & Classification
Click any tag to browse matching papers- Citations
- 8
- FWCI
- 0.45
- Field percentile
- 47th percentile
- Assay
- Research Focus
- Approach
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- Can we put Humpty Dumpty back together again? What does protein quantification mean in bottom-up proteomics?
D. L. Plubell, L. Käll, … M. J. MacCoss·bioRxiv·Jan 25, 2021
- PEPerMINT: Peptide Abundance Imputation in Mass Spectrometry-based Proteomics using Graph Neural Networks
Tobias Pietz, Sukrit Gupta, … Katharina Baum·BioinformaticsPeer-reviewed·Jun 17, 2024
- PeptideForest: Semisupervised machine learning integrating multiple search engines for peptide identification
Tristan Ranff, Matthew Dennison, … Christian Fufezan·Journal of Proteome ResearchPeer-reviewed·Jan 22, 2025
- Leveraging the Human Panproteome to Enhance Peptide and Protein Identification in Proteomics and Metaproteomics
Jamie Canderan, Ruoying Yuan, … Yuzhen Ye·bioRxiv·Nov 25, 2024
- A UNIQUOME BASED METHOD FOR THE PROTEIN IDENTIFICATION BY MASS SPECTROMETRY
Vasileios Pierros, Evangelos Kontopodis, … George Th. Tsangaris·bioRxiv·Oct 8, 2025
- Peptide partitions and protein identification: a computational analysis
G. Sampath·bioRxiv·Aug 14, 2016