Evaluating de novo sequencing in proteomics: already an accurate alternative to database-driven peptide identification?
peer-reviewed · Briefings in Bioinformatics · 2017
| Date | 2017-03-21 |
| Type | peer-reviewed |
| Venue | Briefings in Bioinformatics |
| Publisher | Oxford University Press |
| Contribution | review |
| DOI | 10.1093/bib/bbx033 |
| Citations (OpenAlex) | 129 |
| Venue 2-year citedness | 6.23 |
Abstract
While peptide identifications in mass spectrometry (MS)-based shotgun proteomics are mostly obtained using database search methods, high-resolution spectrum data from modern MS instruments nowadays offer the prospect of improving the performance of computational de novo peptide sequencing. The major benefit of de novo sequencing is that it does not require a reference database to deduce full-length or partial tag-based peptide sequences directly from experimental tandem mass spectrometry spectra. Although various algorithms have been developed for automated de novo sequencing, the prediction accuracy of proposed solutions has been rarely evaluated in independent benchmarking studies. The main objective of this work is to provide a detailed evaluation on the performance of de novo sequencing algorithms on high-resolution data. For this purpose, we processed four experimental data sets acquired from different instrument types from collision-induced dissociation and higher energy collisional dissociation (HCD) fragmentation mode using the software packages Novor, PEAKS and PepNovo. Moreover, the accuracy of these algorithms is also tested on ground truth data based on simulated spectra generated from peak intensity prediction software. We found that Novor shows the overall best performance compared with PEAKS and PepNovo with respect to the accuracy of correct full peptide, tag-based and single-residue predictions. In addition, the same tool outpaced the commercial competitor PEAKS in terms of running time speedup by factors of around 12-17. Despite around 35% prediction accuracy for complete peptide sequences on HCD data sets, taken as a whole, the evaluated algorithms perform moderately on experimental data but show a significantly better performance on simulated data (up to 84% accuracy). Further, we describe the most frequently occurring de novo sequencing errors and evaluate the influence of missing fragment ion peaks and spectral noise on the accuracy. Finally, we discuss the potential of de novo sequencing for now becoming more widely used in the field.
Methods and tools
- Evaluating de novo sequencing vs database-driven identification: Briefings in Bioinformatics review evaluating whether de novo sequencing has become an accurate alternative to database-driven peptide identification. Surveys state-of-the-art tools and benchmark performance circa 2017.
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- Zero-shot de novo peptide sequencing with open posttranslational modification discovery (2026) crossref
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- Modanovo: A Unified Model for Post-translational Modification-Aware De Novo Sequencing Using Experimental Spectra From In Vivo and Synthetic Peptides (2025) both
- Identification of Unknown Biological Toxin Proteins Using Mass Spectrometry: A Case Study on De Novo Sequencing of Ricin (2025) both
- Modanovo: A Unified Model for Post-Translational Modification-Aware de Novo Sequencing Using Experimental Spectra from In Vivo and Synthetic Peptides (2025) crossref
- Limitations of de novo sequencing in resolving sequence ambiguity (2025) crossref
- MARLOWE: Taxonomic Characterization of Unknown Samples for Forensics Using De Novo Peptide Identification (2025) crossref
- InstaNovo enables diffusion-powered de novo peptide sequencing in large-scale proteomics experiments (2025) both
- DiNovo: high-coverage, high-confidence de novo peptide sequencing using mirror proteases and deep learning (2025) crossref
- Metaproteomics Beyond Databases: Addressing the Challenges and Potentials of De Novo Sequencing (2025) crossref
- MARS an improved de novo peptide candidate selection method for non-canonical antigen target discovery in cancer (2024) both
- Deep learning-driven fragment ion series classification enables highly precise and sensitive de novo peptide sequencing (2024) both
- Mitigating the missing-fragmentation problem in de novo peptide sequencing with a two-stage graph-based deep learning model (2023) both
- De novo peptide sequencing with InstaNovo: Accurate, database-free peptide identification for large scale proteomics experiments (2023) both
- Algorithms for de-novo sequencing of peptides by tandem mass spectrometry: A review (2023) crossref
- Denovo-GCN: De Novo Peptide Sequencing by Graph Convolutional Neural Networks (2023) both
- Multienzyme deep learning models improve peptide de novo sequencing by mass spectrometry proteomics (2023) both
- Comprehensive evaluation of peptide de novo sequencing tools for monoclonal antibody assembly (2023) both
- Deep learning-driven fragment ion series classification enables highly precise and sensitive de novo peptide sequencing (2023) crossref
- DePS: An improved deep learning model for de novo peptide sequencing (2022) semanticscholar
- Highly Robust de Novo Full-Length Protein Sequencing (2021) both
- Flying blind, or just flying under the radar? The underappreciated power of de novo methods of mass spectrometric peptide identification (2020) crossref
- Deep Learning in Proteomics (2020) both
- Extended Snake Venomics by Top-Down In-Source Decay: Investigating the Newly Discovered Anatolian Meadow Viper Subspecies, Vipera anatolica senliki (2020) both
- pNovo 3: precise de novo peptide sequencing using a learning-to-rank framework (2019) both
- Postnovo: Postprocessing Enables Accurate and FDR-Controlled de Novo Peptide Sequencing (2018) crossref
- pSite: Amino Acid Confidence Evaluation for Quality Control of De Novo Peptide Sequencing and Modification Site Localization (2017) crossref