Mass Spectrometry-Based Structural Analysis of Cysteine-Rich Metal-Binding Sites in Proteins with MetaOdysseus R Software

Simple item page
dc.contributor"European Union (EU)" & "Horizon 2020"en
dc.contributor.authorPeris-Díaz, Manuel Davidcs
dc.contributor.authorGuráň, Romancs
dc.contributor.authorZítka, Ondřejcs
dc.contributor.authorAdam, Vojtěchcs
dc.contributor.authorKrężel, Arturcs
dc.coverage.issue1cs
dc.coverage.volume20cs
dc.date.accessioned2020-11-09T11:54:41Z
dc.date.available2020-11-09T11:54:41Z
dc.date.issued2021-01-01cs
dc.description.abstractIdentification of metal-binding sites in proteins and understanding metalcoupled protein folding mechanisms are aspects of high importance for the structure-tofunction relationship. Mass spectrometry (MS) has brought a powerful adjunct perspective to structural biology, obtaining from metal-to-protein stoichiometry to quaternary structure information. Currently, the different experimental and/or instrumental setups usually require the use of multiple data analysis software, and in some cases, they lack some of the main data analysis steps (MS processing, scoring, identification). Here, we present a comprehensive data analysis pipeline that addresses charge-state deconvolution, statistical scoring, and mass assignment for native MS, bottom-up, and native top-down with emphasis on metalprotein complexes. We have evaluated all of the approaches using assemblies of increasing complexity, including free and chemically labeled proteins, from low- to high-resolution MS. In all cases, the results have been compared with common software and proved how MetaOdysseus outperformed them.en
dc.formattextcs
dc.format.extent776-785cs
dc.format.mimetypeapplication/pdfcs
dc.identifier.citationJOURNAL OF PROTEOME RESEARCH. 2021, vol. 20, issue 1, p. 776-785.en
dc.identifier.doi10.1021/acs.jproteome.0c00651cs
dc.identifier.issn1535-3893cs
dc.identifier.other165902cs
dc.identifier.urihttp://hdl.handle.net/11012/195634
dc.language.isoencs
dc.publisherAmerican Chemical Societycs
dc.relation.ispartofJOURNAL OF PROTEOME RESEARCHcs
dc.relation.projectIdinfo:eu-repo/grantAgreement/EC/H2020/759585/EU//ToMeTuMen
dc.relation.urihttps://pubs.acs.org/doi/10.1021/acs.jproteome.0c00651cs
dc.rightsCreative Commons Attribution 4.0 Internationalcs
dc.rights.accessopenAccesscs
dc.rights.sherpahttp://www.sherpa.ac.uk/romeo/issn/1535-3893/cs
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/cs
dc.subjectmetalloproteinen
dc.subjectzincen
dc.subjectCys-richen
dc.subjectmass spectrometryen
dc.subjectR packageen
dc.titleMass Spectrometry-Based Structural Analysis of Cysteine-Rich Metal-Binding Sites in Proteins with MetaOdysseus R Softwareen
dc.type.driverarticleen
dc.type.statusPeer-revieweden
dc.type.versionpublishedVersionen
sync.item.dbidVAV-165902en
sync.item.dbtypeVAVen
sync.item.insts2021.03.31 16:55:05en
sync.item.modts2021.03.31 16:14:17en
thesis.grantorVysoké učení technické v Brně. Středoevropský technologický institut VUT. Chytré nanonástrojecs
Files
Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
acs.jproteome.0c00651.pdf
Size:
1.46 MB
Format:
Adobe Portable Document Format
Description:
acs.jproteome.0c00651.pdf
Download
Collections
Chytré nanonástroje