Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8767
Authors: Kwiatkowski, Marcel
Hotze, Madlen
Schumacher, Julia
Asif, Abdul R.
Miguel, Jose
Pittol, Ramos
Brenig, Bertram
Ramljak, Sanja
Zischler, Hans
Herlyn, Holger
Title: Protein speciation is likely to increase the chance of proteins to be determined in 2-DE/MS
Online publication date: 7-Feb-2023
Year of first publication: 2022
Language: english
Abstract: Multiple spotting due to protein speciation might increase a protein's chance of being captured in a random selection of 2-DE spots. We tested this expectation in new (PXD015649) and previously published 2-DE/MS data of porcine and human tissues. For comparison, we included bottom-up proteomics studies (BU-LC/MS) of corresponding biological materials. Analyses of altogether ten datasets proposed that amino acid modification fosters multispotting in 2-DE. Thus, the number of 2-DE spots containing a particular protein more tightly associated with a peptide diversity measure accounting for amino acid modification than with an alternative one disregarding it. Furthermore, every 11th amino acid was a post-translational modification candidate site in 2-DE/MS proteins, whereas in BU-LC/MS proteins this was merely the case in every 21st amino acid. Alternative splicing might contribute to multispotting, since genes encoding 2-DE/MS proteins were found to have on average about 0.3 more transcript variants than their counterparts from BU-LC/MS studies. Correspondingly, resolution completeness as estimated from the representation of transcript variant-rich genes was higher in 2-DE/MS than BU-LC/MS datasets. These findings suggest that the ability to resolve proteomes down to protein species can lead to enrichment of multispotting proteins in 2-DE/MS. Low sensitivity of stains and MS instruments appears to enhance this effect.
DDC: 300 Sozialwissenschaften
300 Social sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 02 Sozialwiss., Medien u. Sport
Place: Mainz
ROR: https://ror.org/023b0x485
DOI: http://doi.org/10.25358/openscience-8767
Version: Published version
Publication type: Zeitschriftenaufsatz
Document type specification: Scientific article
License: CC BY-NC
Information on rights of use: https://creativecommons.org/licenses/by-nc/4.0/
Journal: Electrophoresis
43
11
Pages or article number: 1203
1214
Publisher: John Wiley & Sons, Ltd
Publisher place: Weinheim
Issue date: 2022
ISSN: 1522-2683
Publisher DOI: 10.1002/elps.202000393
Appears in collections:DFG-491381577-H

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