Thema der Dissertation:
Tracking Proton Transfers in the Optogenetic Proteins Channelrhodopsin-1 and DsLOV
Tracking Proton Transfers in the Optogenetic Proteins Channelrhodopsin-1 and DsLOV
Abstract: The field of optogenetics is in constant development while searching for new optogenetic tools that can be used to control nerve cells, stimulus and optical control of neuronal activity. Among the candidates to be developed as new optogenetics tools, are the LOV (Light Oxygen Voltage) proteins which are ubiquitous photosensors in all domains of life. Channelrhodopsins are frequently used in optogenetics due to their light-gated cation activity, which is a unique characteristic among the ion channels.
Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits slower inactivation under continuous illumination and a shift in the visible maximum absorption compared to Channelrhodopsin-1 and Channelrhodopsin-2 from Chlamydomonas reinhardtii. These features are advantageous when developing optogenetic tools, securing CaChR1 as a viable candidate for research. In this work, by variation of amino acid chains, an investigation of the molecular changes in the photocycle of CaChR1 was conducted.
Among the LOV domains an investigation on a variant of the short LOV protein from Dinoroseobacter shibae was conducted. The DsLOV-M49S has the advantage of having an exceptionally fast photocycle compared to other LOV domains. This unique feature of DsLOV-M49S enables the performance of time-resolved molecular spectroscopy and the characterization of the thio-adduct state's formation.
Channelrhodopsin-1 from Chlamydomonas augustae (CaChR1) exhibits slower inactivation under continuous illumination and a shift in the visible maximum absorption compared to Channelrhodopsin-1 and Channelrhodopsin-2 from Chlamydomonas reinhardtii. These features are advantageous when developing optogenetic tools, securing CaChR1 as a viable candidate for research. In this work, by variation of amino acid chains, an investigation of the molecular changes in the photocycle of CaChR1 was conducted.
Among the LOV domains an investigation on a variant of the short LOV protein from Dinoroseobacter shibae was conducted. The DsLOV-M49S has the advantage of having an exceptionally fast photocycle compared to other LOV domains. This unique feature of DsLOV-M49S enables the performance of time-resolved molecular spectroscopy and the characterization of the thio-adduct state's formation.
Zeit & Ort
17.11.2021 | 16:30
Hörsaal A (1.3.14)
Fachbereich Physik, Arnimallee 14, 14195 Berlin
*Die aktuellen Hygieneregelungen sind einzuhalten.*