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dc.contributor.authorSarabi, Daniel
dc.date.accessioned2022-05-11T07:01:08Z
dc.date.available2022-05-11T07:01:08Z
dc.identifier.isbn978-91-8009-851-9
dc.identifier.isbn978-91-8009-852-6
dc.identifier.urihttps://hdl.handle.net/2077/71436
dc.description.abstractLight is one of the most important sources of energy and environmental signals, and many organisms adapt in response to the presence of light. This is made possible through specialised proteins called photoreceptors. Rhodopsins are made light-sensitive via the addition of a retinal chromophore, and activated by specific wavelengths of light, which propagates a cascade of structural changes, allowing the protein to carry out it’s function. Microbial rhodopsins have been found to act as light-driven proton pumps, light-gated ion channels or receptors for phototaxis, whereas rhodopsin in higher eukaryotes such as the human eye, is responsible for low-light vision. Time-resolved X-ray solution scattering (TR-XSS) is a sub-field of structural biology which can detect secondary structural changes in proteins as they evolve along their functional pathways in real time. The method addresses many of the limitations of serial crystallography, however, structural modelling is more challenging due to the measured information being one-dimensional. Further challenges arise in structural interpretation of TR-XSS data recorded from integral membrane proteins, due to the presence of a detergent micelle surrounding the protein. In our previous modelling, the interference between the protein and micelle was not addressed, and in this thesis we utilize molecular dynamics simulations to explicitly incorporate the X-ray scattering cross-term between an integral membrane protein and it’s surrounding micelle when modelling against TR-XSS data from photo-activated rhodopsins within a detergent micelle. The influence of the detergent micelle and micelle size on difference X-ray scattering was determined, correction for the solvent excluded volume was made and candidate motions were identified using these protocols for modelling against TR-XSS data of bacteriorhodopsin, SRII in isolation and in complex with it’s transducer protein HrII, and Channelrhodopsin 2. The analysis tools and protocols developed in this thesis should provide a framework for the analysis and structural modelling of light-activated integral membrane proteins as a powerful complement to other biophysical methods.en_US
dc.language.isoengen_US
dc.relation.haspartPAPER I Sarabi,D., Ostojić,L., Bosman,R., Vallejos,A., Linse,J., Wulff,M., Levantino,M., Neutze,R. "Modelling differ- ence X-ray scattering observations from an integral membrane protein within a detergent micelle." [Submitted manuscript 2022].en_US
dc.relation.haspartPAPER II Sarabi,D., Bosman,R., Ostojić,L., Ghosh,S., Ortolani,G., Levantino,M., Pedersen,M., Sander,M., Båth,P., Dods,R., Hammarin,G., Safari,C., Wulff,M., Brändén,G., Neutze,R. "Time resolved X-ray scattering observations of light-induced structural changes in Sensory Rhodopsin II." [Unpublished manuscript 2022].en_US
dc.relation.haspartPAPER III Sarabi,D., Ortolani,G., Wickstrand,C., Ostojić,L., Ghosh,S., Bosman,R., Pedersen,M., Sander,M., Båth,P., Dods,R., Hammarin,G., Safari,C., Levantino,M., Wulff,M., Brändén,G., Neutze,R. "Time-resolved X-ray solution scattering studies of structural changes in Channelrhodopsin 2." [Unpublished manuscript 2022].en_US
dc.subjectStructural Biologyen_US
dc.subjectTime-resolved X-ray solution scatteringen_US
dc.subjectRhodopsinsen_US
dc.subjectMolecular Dynamicsen_US
dc.subjectProtein dynamicsen_US
dc.titleStructural Dynamics of Rhodopsins using Time-Resolved X-ray Solution Scatteringen_US
dc.typeTextswe
dc.type.svepDoctoral thesiseng
dc.gup.maildaniel.sarabi@gu.seen_US
dc.type.degreeDoctor of Philosophyen_US
dc.gup.originUniversity of Gothenburg.Faculty of Science.en_US
dc.gup.departmentDepartment of Chemistry and Molecular Biology ; Institutionen för kemi och molekylärbiologien_US
dc.gup.defenceplaceOnsdagen den 15 juni 2022, kl 9.00, Hörsal 2119, Hälsovetarbacken, Sahlgrenska Akademin, Arvid Wallgrens backe 5,Göteborg.en_US
dc.gup.defencedate2022-06-15
dc.gup.dissdb-fakultetMNF


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