Leveraging parameter dependencies in high-field asymmetric waveform ion-mobility spectrometry and size exclusion chromatography for proteome-wide cross-linking mass spectrometry

dc.contributor.authorSinn, Ludwig R.
dc.contributor.authorGiese, Sven H.
dc.contributor.authorStuiver, Marchel
dc.contributor.authorRappsilber, Juri
dc.date.accessioned2022-10-12T11:07:45Z
dc.date.available2022-10-12T11:07:45Z
dc.date.issued2022-03-11
dc.description.abstractIon-mobility spectrometry shows great promise to tackle analytically challenging research questions by adding another separation dimension to liquid chromatography–mass spectrometry. The understanding of how analyte properties influence ion mobility has increased through recent studies, but no clear rationale for the design of customized experimental settings has emerged. Here, we leverage machine learning to deepen our understanding of field asymmetric waveform ion-mobility spectrometry for the analysis of cross-linked peptides. Knowing that predominantly m/z and then the size and charge state of an analyte influence the separation, we found ideal compensation voltages correlating with the size exclusion chromatography fraction number. The effect of this relationship on the analytical depth can be substantial as exploiting it allowed us to almost double unique residue pair detections in a proteome-wide cross-linking experiment. Other applications involving liquid- and gas-phase separation may also benefit from considering such parameter dependencies.en
dc.description.sponsorshipDFG, 390540038, EXC 2008: Unifying Systems in Catalysis "UniSysCat"
dc.description.sponsorshipDFG, 392923329, GRK 2473: Bioaktive Peptide - Innovative Aspekte zur Synthese und Biosynthese
dc.identifier.eissn1520-6882
dc.identifier.issn0003-2700
dc.identifier.urihttps://depositonce.tu-berlin.de/handle/11303/17570
dc.identifier.urihttps://doi.org/10.14279/depositonce-16351
dc.language.isoen
dc.relation.ispartof10.14279/depositonce-15535
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subject.ddc572 Biochemiede
dc.subject.ddc543 Analytische Chemiede
dc.subject.otherchromatographyen
dc.subject.otherliquid chromatographyen
dc.subject.othernucleic acid structureen
dc.subject.otherpeptides and proteinsen
dc.subject.otherprecursorsen
dc.titleLeveraging parameter dependencies in high-field asymmetric waveform ion-mobility spectrometry and size exclusion chromatography for proteome-wide cross-linking mass spectrometryen
dc.typeArticle
dc.type.versionpublishedVersion
dcterms.bibliographicCitation.doi10.1021/acs.analchem.1c04373
dcterms.bibliographicCitation.issue11
dcterms.bibliographicCitation.journaltitleAnalytical Chemistry
dcterms.bibliographicCitation.originalpublishernameAmerican Chemical Society
dcterms.bibliographicCitation.originalpublisherplaceColumbus, Ohio
dcterms.bibliographicCitation.pageend4634
dcterms.bibliographicCitation.pagestart4627
dcterms.bibliographicCitation.volume94
tub.accessrights.dnbfree
tub.affiliationFak. 3 Prozesswissenschaften::Inst. Biotechnologie::FG Bioanalytik
tub.publisher.universityorinstitutionTechnische Universität Berlin

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