Power and limitations of electrophoretic separations in proteomics strategies
Thierry Rabilloud (BBSI), Ali R Vaezzadeh, Noelle Potier, C\'ecile, Lelong (BBSI), Emmanuelle Leize-Wagner, Mireille Chevallet (BBSI)

TL;DR
This review critically examines electrophoretic separation techniques in proteomics, discussing their principles, applications, and specific features that influence their integration with mass spectrometry for large-scale protein analysis.
Contribution
It provides a comprehensive overview of electrophoretic methods in proteomics, highlighting their capabilities and limitations in the context of large-scale protein analysis.
Findings
Electrophoretic techniques are essential for protein separation prior to mass spectrometry.
Gel electrophoresis has unique features affecting protein detection and peptide recovery.
The review discusses the interplay between electrophoresis and mass spectrometry in proteomics.
Abstract
Proteomics can be defined as the large-scale analysis of proteins. Due to the complexity of biological systems, it is required to concatenate various separation techniques prior to mass spectrometry. These techniques, dealing with proteins or peptides, can rely on chromatography or electrophoresis. In this review, the electrophoretic techniques are under scrutiny. Their principles are recalled, and their applications for peptide and protein separations are presented and critically discussed. In addition, the features that are specific to gel electrophoresis and that interplay with mass spectrometry (i.e., protein detection after electrophoresis, and the process leading from a gel piece to a solution of peptides) are also discussed.
Peer Reviews
No public reviews on file for this paper yet. If you reviewed it on a platform where reviews are public (OpenReview, ICLR, NeurIPS, ICML), you can paste yours below so the community can read it here.
Videos
No videos yet. Explain this paper in a talk, walkthrough, or lecture? Add one.
