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dc.contributor.authorWard, Richard
dc.contributor.authorPliotas, Christos
dc.contributor.authorBranigan, Emma
dc.contributor.authorHacker, Christian
dc.contributor.authorRasmussen, Akiko
dc.contributor.authorHagelueken, Gregor
dc.contributor.authorBooth, Ian R
dc.contributor.authorMiller, Samantha
dc.contributor.authorLucocq, John
dc.contributor.authorNaismith, Jim
dc.contributor.authorSchiemann, Olav
dc.date.accessioned2014-05-14T09:01:03Z
dc.date.available2014-05-14T09:01:03Z
dc.date.issued2014-02-18
dc.identifier.citationWard , R , Pliotas , C , Branigan , E , Hacker , C , Rasmussen , A , Hagelueken , G , Booth , I R , Miller , S , Lucocq , J , Naismith , J & Schiemann , O 2014 , ' Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance ' , Biophysical Journal , vol. 106 , no. 4 , pp. 834-842 . https://doi.org/10.1016/j.bpj.2014.01.008en
dc.identifier.issn0006-3495
dc.identifier.otherPURE: 100692808
dc.identifier.otherPURE UUID: 61c5215a-60db-4677-9ecd-67cf7892ad36
dc.identifier.otherScopus: 84894494035
dc.identifier.otherORCID: /0000-0002-4309-4858/work/31524148
dc.identifier.otherWOS: 000331674700011
dc.identifier.otherORCID: /0000-0002-5191-0093/work/64361247
dc.identifier.urihttp://hdl.handle.net/10023/4780
dc.descriptionFunding: EaStCHEM studentship to E.B. The work was funded by BBSRC grant BB/H017917/1 to JNH, OS & IRB, The Leverhulme Foundation (EM-2012-60\2) and equipment from a Wellcome Trust Capital Award.en
dc.description.abstractMechanosensitive channel proteins are important safety valves against osmotic shock in bacteria, and are involved in sensing touch and sound waves in higher organisms. The mechanosensitive channel of small conductance (MscS) has been extensively studied. Pulsed electron-electron double resonance (PELDOR or DEER) of detergent-solubilized protein confirms that as seen in the crystal structure, the outer ring of transmembrane helices do not pack against the pore- forming helices, creating an apparent void. The relevance of this void to the functional form of MscS in the bilayer is the subject of debate. Here, we report PELDOR measurements of MscS reconstituted into two lipid bilayer systems: nanodiscs and bicelles. The distance measurements from multiple mutants derived from the PELDOR data are consistent with the detergent-solution arrangement of the protein. We conclude, therefore, that the relative positioning of the transmembrane helices is preserved in mimics of the cell bilayer, and that the apparent voids are not an artifact of detergent solution but a property of the protein that will have to be accounted for in any molecular mechanism of gating.
dc.format.extent9
dc.language.isoeng
dc.relation.ispartofBiophysical Journalen
dc.rightsCopyright © 2014 The Authors. This is an Open Access article distributed under the terms of the Creative Commons-Attribution Noncommercial License (http://creativecommons.org/licenses/by-nc/2.0/), which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited.en
dc.subjectQD Chemistryen
dc.subjectQH301 Biologyen
dc.subjectBDCen
dc.subject.lccQDen
dc.subject.lccQH301en
dc.titleProbing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonanceen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews.School of Biologyen
dc.contributor.institutionUniversity of St Andrews.School of Chemistryen
dc.contributor.institutionUniversity of St Andrews.School of Medicineen
dc.contributor.institutionUniversity of St Andrews.Biomedical Sciences Research Complexen
dc.contributor.institutionUniversity of St Andrews.EaSTCHEMen
dc.identifier.doihttps://doi.org/10.1016/j.bpj.2014.01.008
dc.description.statusPeer revieweden
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/24559986en


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