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Synthesis of Rigid Spin Labels for the Investigation of Transmembrane Peptides by EPR Spectroscopy

dc.contributor.advisorDiederichsen, Ulf Prof. Dr.
dc.contributor.authorWegner, Janine
dc.date.accessioned2018-04-27T09:04:13Z
dc.date.available2018-04-27T09:04:13Z
dc.date.issued2018-04-27
dc.identifier.urihttp://hdl.handle.net/11858/00-1735-0000-002E-E3CF-C
dc.identifier.urihttp://dx.doi.org/10.53846/goediss-6854
dc.language.isoengde
dc.publisherNiedersächsische Staats- und Universitätsbibliothek Göttingende
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subject.ddc540de
dc.titleSynthesis of Rigid Spin Labels for the Investigation of Transmembrane Peptides by EPR Spectroscopyde
dc.typedoctoralThesisde
dc.contributor.refereeDiederichsen, Ulf Prof. Dr.
dc.date.examination2018-02-28
dc.description.abstractengTransmembrane model peptides enable the investigation of complex protein-lipid interactions since the specific structure of proteins is influenced by the lipid environment. Herein, the synthesis of nitroxide spin labels for transmembrane peptides is present and PEDLOR nanometer distance measurements are discussed. It was demonstrated that the combination of semi-rigid labels with high-power pulsed EPR allows straightforward structural interpretation of the observed distances in solution and lipid bilayer. In particular, the labels deliver reliable distances and sharp distance distributions even in the lipid bilayer.de
dc.contributor.coRefereeBennati, Marina Prof. Dr.
dc.subject.engnitroxide radicalde
dc.subject.engspin labelde
dc.subject.engtransmembrane peptidesde
dc.subject.engEPRde
dc.subject.engPELDORde
dc.subject.engmembranede
dc.identifier.urnurn:nbn:de:gbv:7-11858/00-1735-0000-002E-E3CF-C-2
dc.affiliation.instituteFakultät für Chemiede
dc.subject.gokfullChemie  (PPN62138352X)de
dc.identifier.ppn1022271830


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