Show simple item record

Files in this item

Thumbnail

Item metadata

dc.contributor.authorWort, Joshua L.
dc.contributor.authorAckermann, Katrin
dc.contributor.authorGiannoulis, Angeliki
dc.contributor.authorStewart, Alan J.
dc.contributor.authorNorman, David G.
dc.contributor.authorBode, Bela E.
dc.date.accessioned2019-08-16T16:30:03Z
dc.date.available2019-08-16T16:30:03Z
dc.date.issued2019-08-19
dc.identifier260618369
dc.identifier2774d1b0-fe97-4d6a-8092-66840d165160
dc.identifier85069937480
dc.identifier000480287500018
dc.identifier.citationWort , J L , Ackermann , K , Giannoulis , A , Stewart , A J , Norman , D G & Bode , B E 2019 , ' Sub-micromolar pulse dipolar EPR spectroscopy reveals increasing Cu II -labelling of double-histidine motifs with lower temperature ' , Angewandte Chemie - International Edition , vol. 58 , no. 34 , pp. 11681-11685 . https://doi.org/10.1002/anie.201904848en
dc.identifier.issn1433-7851
dc.identifier.otherORCID: /0000-0003-4580-1840/work/60630673
dc.identifier.otherORCID: /0000-0002-3384-271X/work/60630825
dc.identifier.urihttps://hdl.handle.net/10023/18326
dc.description.abstractElectron paramagnetic resonance (EPR) distance measurements are making increasingly important contributions to the studies of biomolecules by providing highly accurate geometric constraints. Combining double-histidine motifs with CuII spin labels can further increase the precision of distance measurements. It is also useful for proteins containing essential cysteines that can interfere with thiol-specific labelling. However, the non-covalent CuII coordination approach is vulnerable to low binding-affinity. Herein, dissociation constants (KD) are investigated directly from the modulation depths of relaxation-induced dipolar modulation enhancement (RIDME) EPR experiments. This reveals low- to sub-μm CuII KDs under EPR distance measurement conditions at cryogenic temperatures. We show the feasibility of exploiting the double-histidine motif for EPR applications even at sub-μm protein concentrations in orthogonally labelled CuII–nitroxide systems using a commercial Q-band EPR instrument.
dc.format.extent5
dc.format.extent1497312
dc.language.isoeng
dc.relation.ispartofAngewandte Chemie - International Editionen
dc.subjectDissociation constanten
dc.subjectDouble-histidine motifen
dc.subjectEPR spectroscopyen
dc.subjectNon-covalent interactionsen
dc.subjectRIDMEen
dc.subjectQD Chemistryen
dc.subjectCatalysisen
dc.subjectChemistry(all)en
dc.subjectNDASen
dc.subject.lccQDen
dc.titleSub-micromolar pulse dipolar EPR spectroscopy reveals increasing CuII-labelling of double-histidine motifs with lower temperatureen
dc.typeJournal articleen
dc.contributor.sponsorBBSRCen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. School of Medicineen
dc.contributor.institutionUniversity of St Andrews. Institute of Behavioural and Neural Sciencesen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. Cellular Medicine Divisionen
dc.contributor.institutionUniversity of St Andrews. Centre of Magnetic Resonanceen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.identifier.doi10.1002/anie.201904848
dc.description.statusPeer revieweden
dc.identifier.grantnumberBB/R013780/1en
dc.identifier.grantnumber099149/Z/12/Zen
dc.identifier.grantnumber204821/Z/16/Zen


This item appears in the following Collection(s)

Show simple item record