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dc.contributor.authorRussell, Hannah
dc.contributor.authorStewart, Rachel
dc.contributor.authorPrior, Christopher
dc.contributor.authorOganesyan, Vasily S.
dc.contributor.authorGaule, Thembaninkosi G.
dc.contributor.authorLovett, Janet E.
dc.date.accessioned2021-04-08T11:30:17Z
dc.date.available2021-04-08T11:30:17Z
dc.date.issued2021-03-29
dc.identifier273354547
dc.identifierb667cc4d-7366-4627-8b5e-17c6f7b6ac03
dc.identifier85103353718
dc.identifier000634626900001
dc.identifier.citationRussell , H , Stewart , R , Prior , C , Oganesyan , V S , Gaule , T G & Lovett , J E 2021 , ' DEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformis ' , Applied Magnetic Resonance , vol. First Online . https://doi.org/10.1007/s00723-021-01321-6en
dc.identifier.issn0937-9347
dc.identifier.otherORCID: /0000-0002-3561-450X/work/92020067
dc.identifier.urihttps://hdl.handle.net/10023/22985
dc.descriptionAuthors acknowledge financial support from EPSRC (studentship to HR EP/R513337/1, Grant support to VSO EP/P007554/1, Grant support to TGG EP/L015005/1), The Royal Society (URF to JEL URF150698), and The Wellcome Trust for a multi-user equipment grant (099149/Z/12/Z).en
dc.description.abstractIn the study of biological structures, pulse dipolar spectroscopy (PDS) is used to elucidate spin–spin distances at nanometre-scale by measuring dipole–dipole interactions between paramagnetic centres. The PDS methods of Double Electron Electron Resonance (DEER) and Relaxation Induced Dipolar Modulation Enhancement (RIDME) are employed, and their results compared, for the measurement of the dipolar coupling between nitroxide spin labels and copper-II (Cu(II)) paramagnetic centres within the copper amine oxidase from Arthrobacter globiformis (AGAO). The distance distribution results obtained indicate that two distinct distances can be measured, with the longer of these at c.a. 5 nm. Conditions for optimising the RIDME experiment such that it may outperform DEER for these long distances are discussed. Modelling methods are used to show that the distances obtained after data analysis are consistent with the structure of AGAO.
dc.format.extent21
dc.format.extent967748
dc.language.isoeng
dc.relation.ispartofApplied Magnetic Resonanceen
dc.subjectQC Physicsen
dc.subjectDASen
dc.subject.lccQCen
dc.titleDEER and RIDME measurements of the nitroxide-spin labelled copper-bound amine oxidase homodimer from arthrobacter globiformisen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.institutionUniversity of St Andrews. School of Physics and Astronomyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doi10.1007/s00723-021-01321-6
dc.description.statusPeer revieweden
dc.identifier.urlhttps://link.springer.com/article/10.1007%2Fs00723-021-01321-6#Sec19en
dc.identifier.grantnumber099149/Z/12/Zen


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