Time-resolved and temperature-dependent EPR of conformational dynamics: A spectroscopic view of IGPS, SRII/HtrII and ChR2
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https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-202006103090
https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-202006103090
Titel: | Time-resolved and temperature-dependent EPR of conformational dynamics: A spectroscopic view of IGPS, SRII/HtrII and ChR2 |
Autor(en): | Schumacher, Magdalena |
Erstgutachter: | Prof. Dr. Heinz-Jürgen Steinhoff |
Zweitgutachter: | Prof. Dr. Daniel Kümmel |
Zusammenfassung: | In the present work three different proteins were investigated, namely IGPS, the SRII/HtrII complex and ChR2. EPR spectroscopy combined with SDSL were applied to investigate the relation of the respective protein dynamics and their functions. In case of IGPS spin label side chain dynamics were recorded and allow a classification of loop dynamics during catalysis. For SRII/HtrII an equilibrium of spin label side chain dynamics was found to reflect the equilibrium of the activated and deactivated states, which are responsible for signal transfer through the complex. Time-resolved analyses of side chain dynamics and trapping of intermediates of the light-triggered channel ChR2 identified conformational changes to occur during channel function. Thereby, the EPR spectroscopy proves to be a powerful tool to investigate proteins in context of structural changes during their protein function. |
URL: | https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-202006103090 |
Schlagworte: | Electron paramagnetic resonance; Electron spin resonance |
Erscheinungsdatum: | 10-Jun-2020 |
Lizenzbezeichnung: | Attribution-NonCommercial-NoDerivs 3.0 Germany |
URL der Lizenz: | http://creativecommons.org/licenses/by-nc-nd/3.0/de/ |
Publikationstyp: | Dissertation oder Habilitation [doctoralThesis] |
Enthalten in den Sammlungen: | FB06 - E-Dissertationen |
Dateien zu dieser Ressource:
Datei | Beschreibung | Größe | Format | |
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thesis_schumacher.pdf | Präsentationsformat | 45,78 MB | Adobe PDF | thesis_schumacher.pdf Öffnen/Anzeigen |
Diese Ressource wurde unter folgender Copyright-Bestimmung veröffentlicht: Lizenz von Creative Commons