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Pulse dipolar EPR for determining nanomolar binding affinities

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dc.contributor.authorAckermann, Katrin
dc.contributor.authorWort, Joshua
dc.contributor.authorBode, Bela E.
dc.date.accessioned2022-07-21T13:30:11Z
dc.date.available2022-07-21T13:30:11Z
dc.date.issued2022-08-14
dc.identifier.citationAckermann , K , Wort , J & Bode , B E 2022 , ' Pulse dipolar EPR for determining nanomolar binding affinities ' , Chemical Communications , vol. 58 , no. 63 , pp. 8790-8793 . https://doi.org/10.1039/D2CC02360Aen
dc.identifier.issn1359-7345
dc.identifier.otherPURE: 280450644
dc.identifier.otherPURE UUID: 8ff493c6-25e6-4a74-8f7e-10cdc0d1e1a5
dc.identifier.otherORCID: /0000-0002-3384-271X/work/115941493
dc.identifier.otherScopus: 85134594065
dc.identifier.otherWOS: 000825556600001
dc.identifier.urihttp://hdl.handle.net/10023/25684
dc.descriptionThis research was funded, in whole or in part, by the Wellcome Trust (204821/Z/16/Z). BEB and KA acknowledge support by the Leverhulme Trust (RPG-2018–397). JLW acknowledges support by the BBSRC DTP Eastbio. BEB acknowledges equipment funding by BBSRC (BB/R013780/1 and BB/T017740/1).en
dc.description.abstractProtein interaction studies often require very low concentrations and highly sensitive biophysical methods. Here, we demonstrate that pulse dipolar electron paramagnetic resonance spectroscopy allows measuring dissociation constants in the nanomolar range. This approach is appealing for concentration-limited biomolecular systems and medium-to-high-affinity binding studies, demonstrated here at 50 nanomolar protein concentration.
dc.format.extent4
dc.language.isoeng
dc.relation.ispartofChemical Communicationsen
dc.rightsCopyright © 2022 The Author(s). This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.en
dc.subjectQD Chemistryen
dc.subjectDASen
dc.subject.lccQDen
dc.titlePulse dipolar EPR for determining nanomolar binding affinitiesen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorThe Leverhulme Trusten
dc.contributor.sponsorBBSRCen
dc.contributor.sponsorBBSRCen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Institute of Behavioural and Neural Sciencesen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. Centre of Magnetic Resonanceen
dc.identifier.doihttps://doi.org/10.1039/D2CC02360A
dc.description.statusPeer revieweden
dc.identifier.grantnumber204821/Z/16/Zen
dc.identifier.grantnumberen
dc.identifier.grantnumberRPG-2018-397en
dc.identifier.grantnumberBB/R013780/1en
dc.identifier.grantnumberBB/T017740/1en


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