New ProteomeXchange dataset PXD059108

[ProteomeCentral Agent]

Dear ProteomeXchange subscriber, a new ProteomeXchange dataset is being announced. To see more information, click here:

https://proteomecentral.proteomexchange.org/dataset/PXD059108

Summary of dataset

Status: new
Identifier: PXD059108
HostingRepository: PRIDE
Species: Saccharomyces cerevisiae (Baker's yeast)
Title: CE-MS Top Down Proteomics Multi-lab Study
Submitter: Noah Gould
LabHead: Alexander R. Ivanov
Description: A single gene can give rise to multiple functionally distinct forms of protein molecules, called proteoforms, originating from gene mutations, RNA alternative splicing, polymorphisms, and post-translational modifications (PTMs). It is essential to characterize proteins in a proteoform-specific manner to improve our understanding of their role in health and disease. Mass spectrometry (MS)-based top-down proteomics (TDP) has emerged as a powerful tool for the characterization of proteoforms by coupling high-efficiency liquid-phase separation techniques to high-resolution MS and tandem MS (MS/MS). Capillary zone electrophoresis (CZE)-MS is one such separation technique offering unique advantages compared to conventional liquid chromatography (LC)-MS methods, including highly efficient separations of proteoforms based on electrophoretic mobility (µep), minimal sample and solvent consumption, high sensitivity for proteoform detection, and ease of predicting proteoforms’ µ
ep. In this work, research teams from around the world joined forces to validate the robustness and reproducibility of CZE-MS for TDP in both simple and complex model proteoform mixtures, comparing its performance with state-of-the-art LC-MS methods. This study encompasses a full spectrum of commercially available CE-MS interfaces and CE and MS instrumentation amenable to TDP analysis. We provide a repository of CZE-MS methods and detailed experimental protocols for robust, reproducible, and sensitive CE-MS-based TDP analysis that were evaluated by several laboratories. We expect this study will offer the proteomics community an informative resource of ready-to-use experimental CE-MS techniques and a better understanding of the CZE-MS approach and its potential in TDP, which together will accelerate the broad adoption of CZE-MS in protein and proteoform research.

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