Gutenberg Open Science: Protein speciation is likely to increase the chance of proteins to be determined in 2-DE/MS

Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-8767

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DC Field	Value	Language
dc.contributor.author	Kwiatkowski, Marcel	-
dc.contributor.author	Hotze, Madlen	-
dc.contributor.author	Schumacher, Julia	-
dc.contributor.author	Asif, Abdul R.	-
dc.contributor.author	Miguel, Jose	-
dc.contributor.author	Pittol, Ramos	-
dc.contributor.author	Brenig, Bertram	-
dc.contributor.author	Ramljak, Sanja	-
dc.contributor.author	Zischler, Hans	-
dc.contributor.author	Herlyn, Holger	-
dc.date.accessioned	2023-02-07T08:00:07Z	-
dc.date.available	2023-02-07T08:00:07Z	-
dc.date.issued	2022	-
dc.identifier.uri	https://openscience.ub.uni-mainz.de/handle/20.500.12030/8783	-
dc.description.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.	en_GB
dc.description.sponsorship	Gefördert durch die Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 491381577	de
dc.language.iso	eng	de
dc.rights	CC BY-NC	*
dc.rights.uri	https://creativecommons.org/licenses/by-nc/4.0/	*
dc.subject.ddc	300 Sozialwissenschaften	de_DE
dc.subject.ddc	300 Social sciences	en_GB
dc.title	Protein speciation is likely to increase the chance of proteins to be determined in 2-DE/MS	en_GB
dc.type	Zeitschriftenaufsatz	de
dc.identifier.doi	http://doi.org/10.25358/openscience-8767	-
jgu.type.contenttype	Scientific article	de
jgu.type.dinitype	article	en_GB
jgu.type.version	Published version	de
jgu.type.resource	Text	de
jgu.organisation.department	FB 02 Sozialwiss., Medien u. Sport	de
jgu.organisation.number	7910	-
jgu.organisation.name	Johannes Gutenberg-Universität Mainz	-
jgu.rights.accessrights	openAccess	-
jgu.journal.title	Electrophoresis	de
jgu.journal.volume	43	de
jgu.journal.issue	11	de
jgu.pages.start	1203	de
jgu.pages.end	1214	de
jgu.publisher.year	2022	-
jgu.publisher.name	John Wiley & Sons, Ltd	de
jgu.publisher.place	Weinheim	de
jgu.publisher.issn	1522-2683	de
jgu.organisation.place	Mainz	-
jgu.subject.ddccode	300	de
jgu.publisher.doi	10.1002/elps.202000393	de
jgu.organisation.ror	https://ror.org/023b0x485	-
jgu.subject.dfg	Geistes- und Sozialwissenschaften	de
Appears in collections:	DFG-491381577-H

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