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dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorVELOURS, Christophe
dc.contributor.authorZHOU, Jingji
dc.contributor.authorZECCHIN, Paolo
dc.contributor.authorHE, Nisha
dc.contributor.authorSALAMEH, Myriam
dc.contributor.authorGOLINELLI, Marie-Pierre
dc.contributor.authorGOLINELLI-PIMPANEAU, Béatrice
dc.date.accessioned2023-05-15T10:19:05Z
dc.date.available2023-05-15T10:19:05Z
dc.date.issued2022-02-09
dc.identifier.issn2218-273Xen_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182125
dc.description.abstractEnSize Exclusion Chromatography coupled with Multi-Angle Light Scattering (SEC-MALS) is a technique that determines the absolute molar mass (molecular weight) of macromolecules in solution, such as proteins or polymers, by detecting their light scattering intensity. Because SEC-MALS does not rely on the assumption of the globular state of the analyte and the calibration of standards, the molar mass can be obtained for proteins of any shape, as well as for intrinsically disordered proteins and aggregates. Yet, corrections need to be made for samples that absorb light atthe wavelength of the MALS laser, such as iron–sulfur [Fe-S] cluster-containing proteins. We analyze several examples of [2Fe-2S] and [4Fe-4S] cluster-containing proteins, for which various corrections were applied to determine the absolute molar mass of both the apo- and holo-forms. Importantly, the determination of the absolute molar mass of the [2Fe-2S]-containing holo-NEET proteins allowed us to ascertain a change in the oligomerization state upon cluster binding and, thus, to highlight one essential function of the cluster.
dc.language.isoENen_US
dc.rightsAttribution 3.0 United States*
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/us/*
dc.subject.enSEC-MALS
dc.subject.ensize exclusion chromatography
dc.subject.enmulti-angle light scattering
dc.subject.enmolar mass
dc.subject.enmolecular weight
dc.subject.enFe-S cluster
dc.subject.eniron-sulfur cluster
dc.subject.en[Fe-S]-binding protein
dc.subject.enNEET protein
dc.title.enDetermination of the Absolute Molar Mass of [Fe-S]-Containing Proteins Using Size Exclusion Chromatography-Multi-Angle Light Scattering (SEC-MALS)
dc.typeArticle de revueen_US
dc.identifier.doi10.3390/biom12020270en_US
dc.subject.halPhysique [physics]en_US
dc.subject.halSciences du Vivant [q-bio]en_US
bordeaux.journalBiomoleculesen_US
bordeaux.hal.laboratoriesMFP (Laboratoire Microbiologie Fondamentale et Pathogénicité) - UMR 5234en_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcehal
hal.identifierhal-03563208
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccCC BYen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Biomolecules&rft.date=2022-02-09&rft.eissn=2218-273X&rft.issn=2218-273X&rft.au=VELOURS,%20Christophe&ZHOU,%20Jingji&ZECCHIN,%20Paolo&HE,%20Nisha&SALAMEH,%20Myriam&rft.genre=article


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