Time-Resolved EPR Spectroscopy of Channelrhodopsin-2 Helix B Movements
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Schumacher, Magdalena | |
dc.contributor.author | Bamann, Christian | |
dc.contributor.author | Steinhoff, Heinz-Jürgen | |
dc.date.accessioned | 2024-01-04T10:29:02Z | - |
dc.date.available | 2024-01-04T10:29:02Z | - |
dc.date.issued | 2023 | |
dc.identifier.issn | 0937-9347 | |
dc.identifier.uri | http://osnascholar.ub.uni-osnabrueck.de/handle/unios/72960 | - |
dc.description | Cited by: 0; All Open Access, Hybrid Gold Open Access | |
dc.description.abstract | The light-gated dimeric cation channel channelrhodopsin-2 (ChR2) is one of the most important optogenetic tools. Upon light activation ChR2 undergoes conformational changes, the most prominent ones include a movement of transmembrane helix B. In the present work, we apply time resolved continuous wave EPR spectroscopy to follow spectral changes of a spin label bound to position C79 located in helix B. We observed an increase of the motional freedom of the spin label side chain in illuminated ChR2. The recovery of the underlying light-induced conformational change in the dark is correlated with the recovery of the P480 state of ChR2. The observed conformational changes might be thus key elements responsible for desensitizing the channel for cation conduction. © 2023, The Author(s). | |
dc.language.iso | en | |
dc.publisher | Springer | |
dc.relation.ispartof | Applied Magnetic Resonance | |
dc.subject | Electron spin resonance spectroscopy | |
dc.subject | Paramagnetic resonance | |
dc.subject | Time-resolved spectroscopy | |
dc.subject | Cation channels | |
dc.subject | Conformational change | |
dc.subject | Dimeric cation | |
dc.subject | EPR spectroscopy | |
dc.subject | Light activation | |
dc.subject | Optogenetics | |
dc.subject | Spin label | |
dc.subject | Time-resolved | |
dc.subject | Time-resolved EPR | |
dc.subject | Transmembrane helix | |
dc.subject | Positive ions | |
dc.title | Time-Resolved EPR Spectroscopy of Channelrhodopsin-2 Helix B Movements | |
dc.type | journal article | |
dc.identifier.doi | 10.1007/s00723-023-01612-0 | |
dc.identifier.scopus | 2-s2.0-85171432895 | |
dc.identifier.url | https://www.scopus.com/inward/record.uri?eid=2-s2.0-85171432895&doi=10.1007%2fs00723-023-01612-0&partnerID=40&md5=90e6c34c4ec3901c03b1dc48e344ecdf | |
dcterms.isPartOf.abbreviation | Appl. Magn. Reson. | |
local.import.remains | affiliations : Universität Osnabrück, Barbarastrasse 7, Osnabrück, 49076, Germany; Abteilung für Biophysikalische Chemie, Max-Planck-Institut für Biophysik, Max-von-Laue Str. 3, Frankfurt a. M., 60438, Germany | |
local.import.remains | correspondence_address : H.-J. Steinhoff; Universität Osnabrück, Osnabrück, Barbarastrasse 7, 49076, Germany; email: hsteinho@uni-osnabrueck.de | |
local.import.remains | publication_stage : Article in press | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
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geprüft am 06.06.2024