| dc.contributor.author | Malmerberg, Erik | |
| dc.date.accessioned | 2011-10-27T07:57:02Z | |
| dc.date.available | 2011-10-27T07:57:02Z | |
| dc.date.issued | 2011-10-27 | |
| dc.identifier.isbn | 978-91-628-8371-3 | |
| dc.identifier.uri | http://hdl.handle.net/2077/27026 | |
| dc.description.abstract | Rhodopsins are a family of light-sensitive proteins found in the cellular membranes of a
wide range of living organisms. These membrane proteins share a common molecular
architecture and are able to use light energy to perform a variety of different biological
functions. Mapping the conformational changes required for these proteins to function is
important for understanding how light energy is used for energy transduction and
sensory perception in biological systems.
In order to visualize these conformational changes over time, the emerging technique of
time-resolved wide angle X-ray scattering (TR-WAXS) was employed. Several technical
and analytical developments of this solution based method were made during the course
of this work, including the development of a new data collection strategy based on a
rapid readout X-ray detector.
The light-driven proton pumps bacteriorhodopsin and proteorhodopsin were the first
membrane proteins to be characterized using TR-WAXS. The results from these studies
indicated that significant α-helical rearrangements precede the primary proton transfer
event in bacteriorhodopsin. Comparison with the evolutionary related proteorhodopsin
provided important insights into shared conformational dynamics between the two
proton-pumps.
Proteorhodopsin was further investigated by probing the conformational changes
occurring within its chromophore binding pocket, where the chromophore of
proteorhodopsin was substituted with a chemically modified retinal analogue.
Comparison between the native and modified form of proteorhodopsin indicated
significant chromophore dependant differences in their conformational kinetics. These
differences provided new insights into the coupling between retinal isomerisation and
protein conformational changes.
The conformational dynamics within visual rhodopsin, the primary light sensor of
vertebrate vision, were also investigated using TR-WAXS. By using the rapid readout X-ray detector we were able to follow the activation of this G-protein coupled receptor in
real-time. Structural analysis further indicated that dramatic conformational changes are
associated with the activation of this receptor. | sv |
| dc.language.iso | eng | sv |
| dc.relation.haspart | Paper I.
Westenhoff, S., Nazarenko, E., Malmerberg, E., Davidsson, J., Katona,
G. and Neutze, R. (2010)
Time-resolved structural studies of protein
reaction dynamics: a smorgasbord of x-ray approaches. Acta Cryst, A66, 207-219.
::doi::10.1107/S0108767309054361 | sv |
| dc.relation.haspart | Paper II.
Andersson, M*., Malmerberg, E*., Westenhoff, S., Katona, G., Cammarata, M., Wohri, AB., Johansson, LC., Ewald, F., Eklund, M..,
Wulff, M., Davidsson, J and Neutze, R. (2009) Structural Dynamics of Light-Driven Proton Pumps. Structure, 17, 1265-1275.
::doi::10.1016/j.str.2009.07.007 | sv |
| dc.relation.haspart | Paper III.
Malmerberg, E., Omran, Z., Hub, JS., Li, X., Katona, G., Westenhoff, S., Johansson, LC., Andersson, M., Cammarata, M., Wulff, M., van der Spoel, D., Davidsson, J., Specht, A. and Neutze, R. (2011)
Time- Resolved WAXS Reveals Accelerated Conformational Changes in Iodoretinal-Substituted Proteorhodopsin. Biophys J,101, 1345-1353.
::doi::10.1016/j.bpj.2011.07.050 | sv |
| dc.relation.haspart | Paper IV.
Westenhoff, S*., Malmerberg, E.*, Arnlund, D., Johansson, L., Nazarenko, E., Cammarata, M., Davidsson, J., Chaptal, V., Abramson, J.,
Katona, G., Menzel, A. and Neutze, R. (2010)
Rapid readout detector captures protein time-resolved WAXS. Nat Methods, 7, 775-776
::doi::10.1038/nmeth1010-775c | sv |
| dc.relation.haspart | Paper V.
Malmerberg, E, Katona, G., Bovee, P., Westenhoff, S., Johansson, LC., Arnlund, D., Nazarenko, E., Menzel, A., de Grip, WJ. and Neutze, R. (2011).
Conformational Activation of Rhodopsin Probed by Time-resolved Wide Angle X-ray Scattering. (manuscript) | sv |
| dc.subject | Time-resolved wide Angle X-ray Scattering | sv |
| dc.subject | Retinylidene proteins | sv |
| dc.subject | Rhodopsin | sv |
| dc.subject | Bacteriorhodopsin | sv |
| dc.subject | Proteorhodopsin | sv |
| dc.title | Conformational Dynamics of Rhodopsins Visualized by Time-resolved Wide Angle X-ray Scattering | sv |
| dc.type | Text | |
| dc.type.svep | Doctoral thesis | |
| dc.gup.mail | erik.malmerberg@chem.gu.se | sv |
| dc.type.degree | Doctor of Philosophy | sv |
| dc.gup.origin | University of Gothenburg. Faculty of Science | sv |
| dc.gup.department | Department of Chemistry ; Institutionen för kemi | sv |
| dc.gup.defenceplace | Fredagen den 18:e november 2011 kl. 09.00 i KB-salen, Institutionen för kemi, Kemigården 4, Göteborg. | sv |
| dc.gup.defencedate | 2011-11-18 | |
| dc.gup.dissdb-fakultet | MNF | |
