Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement
DC Element | Wert | Sprache |
---|---|---|
dc.contributor.author | Klare, Johann P. | |
dc.contributor.author | Bordignon, Enrica | |
dc.contributor.author | Engelhard, Martin | |
dc.contributor.author | Steinhoff, Heinz-Jurgen | |
dc.date.accessioned | 2021-12-23T16:11:48Z | - |
dc.date.available | 2021-12-23T16:11:48Z | - |
dc.date.issued | 2004 | |
dc.identifier.issn | 1474905X | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/9893 | - |
dc.description.abstract | EPR spectroscopy in combination with site directed spin labeling (SDSL) has become a valuable tool for structural investigations as well as for kinetic studies on proteins. This method has been especially useful for membrane proteins in yielding structural and functional data. This information is not easily available from other techniques, like, e.g., X-ray crystallography or electron microscopy. In the first part of this two part review, the topology of the sensory rhodopsin II/transducer complex (NpSRII/NpHtrII) derived from EPR constraints is compared to that obtained from X-ray crystallography. In the second part, the helix F movement observed for both sensory rhodopsin and bacteriorhodopsin is evaluated and discussed in order to establish a common mechanism after photoreceptor activation. | |
dc.description.sponsorship | Max Planck SocietyMax Planck SocietyFoundation CELLEX; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [SFB 431/P18]; The financial support of the Max Planck Society (M.E.) and the Deutsche Forschungsgemeinschaft (M.E.; SFB 431/P18, E.B. and H.-J.S.) is gratefully acknowledged. | |
dc.language.iso | en | |
dc.publisher | SPRINGERNATURE | |
dc.relation.ispartof | PHOTOCHEMICAL & PHOTOBIOLOGICAL SCIENCES | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Biophysics | |
dc.subject | Chemistry | |
dc.subject | Chemistry, Physical | |
dc.subject | COGNATE TRANSDUCER | |
dc.subject | CONFORMATIONAL-CHANGES | |
dc.subject | MOLECULAR-MECHANISM | |
dc.subject | NATRONOBACTERIUM-PHARAONIS | |
dc.subject | PHARAONIS PHOBORHODOPSIN | |
dc.subject | PROTON TRANSLOCATION | |
dc.subject | STRUCTURAL-CHANGES | |
dc.subject | TIME-RESOLVED DETECTION | |
dc.subject | TRANSIENT MOVEMENT | |
dc.subject | TRANSMEMBRANE HELICES | |
dc.title | Sensory rhodopsin II and bacteriorhodopsin: Light activated helix F movement | |
dc.type | journal article | |
dc.identifier.doi | 10.1039/b402656j | |
dc.identifier.isi | ISI:000695168300008 | |
dc.description.volume | 3 | |
dc.description.issue | 6 | |
dc.description.startpage | 543 | |
dc.description.endpage | 547 | |
dc.contributor.orcid | 0000-0002-5761-5968 | |
dc.contributor.researcherid | C-1428-2009 | |
dc.identifier.eissn | 14749092 | |
dc.publisher.place | CAMPUS, 4 CRINAN ST, LONDON, N1 9XW, ENGLAND | |
dcterms.isPartOf.abbreviation | Photochem. Photobiol. Sci. | |
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 17.05.2024