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dc.contributor.authorKerry, Philip S
dc.contributor.authorTurkington, Hannah L
dc.contributor.authorAckermann, Katrin
dc.contributor.authorJameison, Stephen A
dc.contributor.authorBode, Bela Ernest
dc.identifier.citationKerry , P S , Turkington , H L , Ackermann , K , Jameison , S A & Bode , B E 2014 , ' Analysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurements ' , Journal of Physical Chemistry B , vol. 118 , no. 37 , pp. 10882-10888 .
dc.identifier.otherPURE: 144516402
dc.identifier.otherPURE UUID: abc901cc-1da7-4b9d-a7b0-7347942071ea
dc.identifier.otherPubMed: 25148246
dc.identifier.otherScopus: 84907720780
dc.identifier.otherORCID: /0000-0002-3384-271X/work/27582731
dc.identifier.otherWOS: 000342120100008
dc.descriptionH.L.T. was supported by the University of St Andrews; S.A.J. is supported by the BBSRC, U.K.; P.S.K. is supported by the Medical Research Council, U.K.; B.E.B. is grateful for an EaStCHEM Hirst Academic Fellowship by the School of Chemistry, St Andrews, and funding from the People Programme (Marie Curie Actions) of the European Union’s Seventh Framework Programme [REA 334496]. This work was supported by the Wellcome Trust [099149/Z/12/Z].en
dc.description.abstractPulsed electron-electron double resonance (PELDOR) is an electron paramagnetic resonance (EPR) spectroscopy technique for nanometer distance measurements between paramagnetic centres such as radicals. PELDOR has been recognized as a valuable tool to approach structural questions in biological systems. In this manuscript we demonstrate the value of distance measurements for differentiating competing structural models on the dimerization of the effector domain (ED) of the non-structural protein 1 (NS1) of the influenza A virus. Our results show NS1 to be well amenable to nanometer distance measurements by EPR, yielding high quality data. In combination with mutants perturbing protein dimerization and in silico prediction based on crystal structures we can exclude one of two potential dimerization interfaces. Furthermore, our results lead to a viable hypothesis of a NS1 ED:ED interface which is flexible through rotation around the vector interconnecting the two native cysteines. These results prove the high value of pulse EPR as a complementary method for structural biology.
dc.relation.ispartofJournal of Physical Chemistry Ben
dc.rights© 2014 American Chemical Society. This is an Open Access article distributed in accordance with the terms of the Creative Commons Attribution (CC-BY) license, which permits others to distribute, remix, adapt and build upon this work, for commercial use, provided the original work is properly citeden
dc.subjectQD Chemistryen
dc.titleAnalysis of influenza A virus NS1 dimer interfaces in solution by pulse EPR distance measurementsen
dc.typeJournal articleen
dc.contributor.sponsorThe Wellcome Trusten
dc.contributor.sponsorEuropean Commissionen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. Centre of Magnetic Resonanceen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.description.statusPeer revieweden

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