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Macromolecular interactions in vitro, comparing classical and novel approaches

dc.rights.licenseopenen_US
hal.structure.identifierMicrobiologie Fondamentale et Pathogénicité [MFP]
dc.contributor.authorVELOURS, Christophe
dc.contributor.authorAUMONT-NICAISE, Magali
dc.contributor.authorUEBEL, Stephan
dc.contributor.authorENGLAND, Patrick
dc.contributor.authorVELAZQUEZ-CAMPOY, Adrian
dc.contributor.authorSTROEBEL, David
dc.contributor.authorBEC, Guillaume
dc.contributor.authorSOULE, Pierre
dc.contributor.authorQUÉTARD, Christophe
dc.contributor.authorEBEL, Christine
dc.contributor.authorROUSSEL, Alain
dc.contributor.authorCHARBONNIER, Jean-Baptiste
dc.contributor.authorVARELA, Paloma Fernández
dc.date.accessioned2023-05-23T10:41:54Z
dc.date.available2023-05-23T10:41:54Z
dc.date.created2021
dc.date.issued2021-04-01
dc.identifier.issn0175-7571en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/182259
dc.description.abstractEnBiophysical quantification of protein interactions is central to unveil the molecular mechanisms of cellular processes. Researchers can choose from a wide panel of biophysical methods that quantify molecular interactions in different ways, including both classical and more novel techniques. We report the outcome of an ARBRE-MOBIEU training school held in June 2019 in Gif-sur-Yvette, France (https://mosbio.sciencesconf.org/). Twenty European students benefited from a week’s training with theoretical and practical sessions in six complementary approaches: (1) analytical ultracentrifugation with or without a fluorescence detector system (AUC-FDS), (2) isothermal titration calorimetry (ITC), (3) size exclusion chromatography coupled to multi-angle light scattering (SEC-MALS), (4) bio-layer interferometry (BLI), (5) microscale thermophoresis (MST) and, (6) switchSENSE. They implemented all these methods on two examples of macromolecular interactions with nanomolar affinity: first, a protein–protein interaction between an artificial alphaRep binder, and its target protein, also an alphaRep; second, a protein-DNA interaction between a DNA repair complex, Ku70/Ku80 (hereafter called Ku), and its cognate DNA ligand. We report the approaches used to analyze the two systems under study and thereby showcase application of each of the six techniques. The workshop provided students with improved understanding of the advantages and limitations of different methods, enabling future choices concerning approaches that are most relevant or informative for specific kinds of sample and interaction.
dc.description.sponsorshipInfrastructure Française pour la Biologie Structurale Intégréeen_US
dc.description.sponsorshipEtude de l'ADP-ribosylation d'ADN et de son rôle dans la réponse aux dommages à l'ADN - ANR-18-CE44-0008en_US
dc.description.sponsorshipCaractérisation de la chorégraphie orchestrée par l'hétérodimère Ku sur les cassures double-brin de l'ADN - ANR-20-CE11-0026en_US
dc.language.isoENen_US
dc.subject.enMolecular scale biophysics
dc.subject.enMacromolecular interactions
dc.subject.enArtificial binders
dc.subject.enDouble-stranded DNA breaks repair factors
dc.title.enMacromolecular interactions in vitro, comparing classical and novel approaches
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s00249-021-01517-5en_US
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaireen_US
bordeaux.journalEuropean Biophysics Journalen_US
bordeaux.page313-330en_US
bordeaux.volume50en_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-03224764
hal.version1
hal.exportfalse
workflow.import.sourcehal
dc.rights.ccPas de Licence CCen_US
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=European%20Biophysics%20Journal&rft.date=2021-04-01&rft.volume=50&rft.spage=313-330&rft.epage=313-330&rft.eissn=0175-7571&rft.issn=0175-7571&rft.au=VELOURS,%20Christophe&AUMONT-NICAISE,%20Magali&UEBEL,%20Stephan&ENGLAND,%20Patrick&VELAZQUEZ-CAMPOY,%20Adrian&rft.genre=article


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