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dc.contributor.advisorBode, Bela Ernest
dc.contributor.authorRemmel, Laura
dc.description.abstractThe understanding of the structures, interactions, and functions of biological systems as well as their impact on health and disease is of fundamental importance. Electron paramagnetic resonance (EPR) spectroscopy has become a powerful tool for the investigation of structures and interactions of various systems. If not intrinsically present in the biological system paramagnetic centres can be introduced into the system of interest via site directed spin labelling (SDSL) to enable the use of EPR methods. Pulsed electron-electron double resonance (PELDOR) as well as relaxation-induced dipolar relaxation enhancement (RIDME) measurements exploit the dipole-dipole coupling between paramagnetic centres. Both methods have been used to investigate the distances between two spin labels, giving valuable insight into the structure of the biological systems investigated as well as sparse long-distance restrains used for structure refinement. PELDOR has in addition been used to determine the number of interacting spins, concluding to the number of interacting molecules. In combination with computational methods for structure prediction this opens a wide range of methods for the investigation and understanding of biological structures and structural transitions. The self-multimerisation of a single stranded DNA binding protein could be shown by PELDOR measurements and the flexibility of the system was validated by computational structure prediction. In another project good insight into the tertiary structure of the M3 protein could be gained using a combined approach of computational structure prediction, PELDOR, and RIDME measurements. ¹⁹F electron-nuclear double resonance (ENDOR) measurements enable the investigation of distances between a nitroxide spin label and a ¹⁹F nucleus. The investigation of a fluoride sensing riboswitch by nuclear magnetic resonance (NMR) spectroscopy and PELDOR showing a fluoride-free, a magnesium-stabilised and a fluoride-bound form is shown and an approach for the determination of the fluoride position in the solution structure based on ¹⁹F ENDOR measurements is introduced.en_US
dc.description.sponsorship"This work and the research activities concomitant with it were supported by the Wellcome Trust, the UK Research and Innovation (UKRI), The Royal Society, The Carnegie Trust, the Scottish NMR Users Group (SNUG), the Royal Society of Chemistry (RSC) and the Gesellschaft Deutscher Chemiker(GDCH)."--Fundingen
dc.relationAdvanced biomolecular applications of electron paramagnetic resonance spectroscopy (thesis data) Remmel, L., University of St Andrews, 24 April 2025. DOI:
dc.subjectM3 protein from Streptococcus pyogenesen_US
dc.subjectSSB protein from Saccharolobus solfataricusen_US
dc.subjectFluoride riboswitch from Thermotoga petrophilaen_US
dc.subjectProtein structure predictionen_US
dc.subject.lcshElectron paramagnetic resonance spectroscopyen
dc.titleAdvanced biomolecular applications of electron paramagnetic resonance spectroscopyen_US
dc.contributor.sponsorWellcome Trusten_US
dc.contributor.sponsorUK Research and Innovation (Agency)en_US
dc.contributor.sponsorRoyal Society (Great Britain)en_US
dc.contributor.sponsorCarnegie Trust for the Universities of Scotlanden_US
dc.contributor.sponsorScottish NMR Users Group (SNUG)en_US
dc.contributor.sponsorRoyal Society of Chemistry (RSC)en_US
dc.contributor.sponsorGesellschaft Deutscher Chemiker (GDCh)en_US
dc.type.qualificationnamePhD Doctor of Philosophyen_US
dc.publisher.institutionThe University of St Andrewsen_US
dc.rights.embargoreasonThesis restricted in accordance with University regulations. Restricted until 24th April 2025en

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