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  • 1
    Book
    Book
    Berlin [u.a.] : De Gruyter
    UID:
    b3kat_BV041107608
    Format: XIV, 226 S. , graph. Darst., Ill. , 240 mm x 170 mm
    ISBN: 3110270714 , 9783110270716
    Series Statement: Dahlem Workshop Reports
    Note: Report of the 102nd Dahlem Workshop on Optogenetics. September 2 - 5, 2012 at Freie Universität Berlin
    Additional Edition: Erscheint auch als Online-Ausgabe ISBN 978-3-11-027072-3
    Language: English
    Subjects: Biology
    RVK:
    Keywords: Nervennetz ; Optogenetik ; Aufsatzsammlung
    Author information: Hegemann, Peter 1954-
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  • 2
    UID:
    b3kat_BV000321664
    Format: 161 S. , Ill.
    Note: München, Univ., Diss., 1984
    Language: German
    Keywords: Halobacterium halobium ; Halorhodopsin ; Hochschulschrift
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  • 3
    Article
    Article
    Berlin : Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I
    UID:
    edochu_18452_10020
    ISSN: 0940-0079 , 0940-0079
    Content: Zu den wichtigsten Signalmolekülen in lebenden Zellen gehört cAMP, das grundlegende Prozesse steuert. Wir haben kürzlich mithilfe eines Algenproteins eine neue Methode entwickelt, cAMP durch kurze Lichtblitze in tierischen Zellen und lebenden Tieren zu erzeugen. Bei Fliegen lassen sich damit Verhaltensänderungen an- und wieder abschalten. Die besonders hohe zeitliche Auflösung dieses neuen Lichtgesteuerten „Werkzeugs“ sollte es ermöglichen, die Rolle von cAMP bei komplexen biologischen Fragestellungen besser zu verstehen.
    Content: Not Reviewed
    In: BIOforum, , 2007, ,2007,6, Seiten 46-47, 0940-0079
    Language: German
    URL: Volltext  (kostenfrei)
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  • 4
    UID:
    edochu_18452_10021
    ISSN: 1548-7091 , 1548-7091
    Content: The flagellate Euglena gracilis contains a photoactivated adenylyl cyclase (PAC), consisting of the flavoproteins PACa and PACb. Here we report functional expression of PACs in Xenopus laevis oocytes, HEK293 cells and in Drosophila melanogaster, where neuronal expression yields light-induced changes in behavior. The activity of PACs is strongly and reversibly enhanced by blue light, providing a powerful tool for light-induced manipulation of cAMP in animal cells.
    Content: Peer Reviewed
    In: Nature Methods, , 2007, 4,2006,1, Seiten 39-42, 1548-7091
    Language: English
    URL: Volltext  (kostenfrei)
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  • 5
    UID:
    b3kat_BV024897421
    Format: 42 gez. Bl.
    Note: Heidelberg, Univ., Diss., 1982
    Language: German
    Keywords: Hochschulschrift
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  • 6
    UID:
    edochu_18452_26010
    Format: 1 Online-Ressource (31 Seiten)
    Content: The rhodopsin-guanylyl cyclase from the nematophagous fungus Catenaria anguillulae belongs to a recently discovered class of enzymerhodopsins and may find application as a tool in optogenetics. Here the rhodopsin domain CaRh of the rhodopsin-guanylyl cyclase from Catenaria anguillulae was studied by absorption and emission spectroscopic methods. The absorption cross-section spectrum and excitation wavelength dependent fluorescence quantum distributions of CaRh samples were determined (first absorption band in the green spectral region). The thermal stability of CaRh was studied by long-time attenuation measurements at room temperature (20.5 °C) and refrigerator temperature of 3.5 °C. The apparent melting temperature of CaRh was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 62 ± 2 °C). The photocycle dynamics of CaRh was investigated by sample excitation to the first inhomogeneous absorption band of the CaRhda dark-adapted state around 590 nm (long-wavelength tail), 530 nm (central region) and 470 nm (short-wavelength tail) and following the absorption spectra development during exposure and after exposure (time resolution 0.0125 s). The original protonated retinal Schiff base PRSBall-trans in CaRhda photo-converted reversibly to protonated retinal Schiff base PRSBall-trans,la1 with restructured surroundings (CaRhla1 light-adapted state, slightly blue-shifted and broadened first absorption band, recovery to CaRhda with time constant of 0.8 s) and deprotonated retinal Schiff base RSB13-cis (CaRhla2 light-adapted state, first absorption band in violet to near ultraviolet spectral region, recovery to CaRhda with time constant of 0.35 s). Long-time light exposure of light-adapted CaRhla1 around 590, 530 and 470 nm caused low-efficient irreversible degradation to photoproducts CaRhprod. Schemes of the primary photocycle dynamics of CaRhda and the secondary photocycle dynamics of CaRhla1 are developed.
    Content: Peer Reviewed
    In: International journal of molecular sciences, Basel : Molecular Diversity Preservation International, 18,2017,10
    Language: English
    URL: Volltext  (kostenfrei)
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  • 7
    UID:
    edochu_18452_26152
    Format: 1 Online-Ressource (22 Seiten)
    Content: The retinal photocycle dynamics of the fluorescent voltage sensor QuasAr1 (Archaerhodopsin 3 P60S-T80S-D95H-D106H-F161V mutant from Halorubrum sodomense) in pH 8 Tris buffer was studied. The samples were photoexcited to the first absorption band of the protonated retinal Schiff base (PRSB) Ret_580 (absorption maximum at λmax ≈ 580 nm), and the retinal Schiff base photoisomerization and protonation state changes were followed by absorption spectra recordings during light exposure and after light exposure. Ret_580 turned out to be composed of two protonated retinal Schiff base isomers, namely Ret_580I and Ret_580II. Photoexcitation of Ret_580I resulted in barrier-involved isomerization to Ret_540 (quantum yield ≈ 0.056) and subsequent retinal proton release leading to Ret_410 deprotonated retinal Schiff base (RSB). In the dark, Ret_410 partially recovered to Ret_580I and partially stabilized to irreversible Ret_400 due to apoprotein restructuring (Ret_410 lifetime ≈ 2 h). Photoexcitation of Ret_580II resulted in barrier-involved isomerization to Ret_640 (quantum yield ≈ 0.00135) and subsequent deprotonation to Ret_370 (RSB). In the dark, Ret_370 partially recovered to Ret_580II and partially stabilized to irreversible Ret_350 due to apoprotein restructuring (Ret_370 lifetime ≈ 10 h). Photocycle schemes and reaction coordinate diagrams for Ret_580I and Ret_580II were developed and photocyle parameters were determined.
    Content: Peer Reviewed
    In: International journal of molecular sciences, Basel : Molecular Diversity Preservation International, 21,2019,1
    Language: English
    URL: Volltext  (kostenfrei)
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  • 8
    UID:
    gbv_011532831
    Format: 161 S. , Ill., graph. Darst.
    Note: München, Univ., Diss., 1984
    Language: German
    Keywords: Halobacterium halobium ; Halorhodopsin ; Hochschulschrift
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  • 9
    UID:
    edochu_18452_26139
    Format: 1 Online-Ressource (24 Seiten)
    Content: QuasAr1 is a fluorescent voltage sensor derived from Archaerhodopsin 3 (Arch) of Halorubrum sodomense by directed evolution. Here we report absorption and emission spectroscopic studies of QuasAr1 in Tris buffer at pH 8. Absorption cross-section spectra, fluorescence quantum distributions, fluorescence quantum yields, and fluorescence excitation spectra were determined. The thermal stability of QuasAr1 was studied by long-time attenuation coefficient measurements at room temperature (23 ± 2 °C) and at 2.5 ± 0.5 °C. The apparent melting temperature was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 65 ± 3 °C). In the protein melting process the originally present protonated retinal Schiff base (PRSB) with absorption maximum at 580 nm converted to de-protonated retinal Schiff base (RSB) with absorption maximum at 380 nm. Long-time storage of QuasAr1 at temperatures around 2.5 °C and around 23 °C caused gradual protonated retinal Schiff base isomer changes to other isomer conformations, de-protonation to retinal Schiff base isomers, and apoprotein structure changes showing up in ultraviolet absorption increase. Reaction coordinate schemes are presented for the thermal protonated retinal Schiff base isomerizations and deprotonations in parallel with the dynamic apoprotein restructurings.
    Content: Peer Reviewed
    In: International journal of molecular sciences, Basel : Molecular Diversity Preservation International, 20,2019,17
    Language: English
    URL: Volltext  (kostenfrei)
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  • 10
    UID:
    edochu_18452_26148
    Content: Archon2 is a fluorescent voltage sensor derived from Archaerhodopsin 3 (Arch) of Halorubrum sodomense using robotic multidimensional directed evolution approach. Here we report absorption and emission spectroscopic studies of Archon2 in Tris buffer at pH 8. Absorption cross-section spectra, fluorescence quantum distributions, fluorescence quantum yields, and fluorescence excitation spectra were determined. The thermal stability of Archon2 was studied by long-time attenuation coefficient measurements at room temperature (21 ± 1 °C) and at refrigerator temperature (3 ± 1 °C). The apparent melting temperature was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 63 ± 3 °C). In the protein melting process protonated retinal Schiff base (PRSB) with absorption maximum at 586 nm converted to de-protonated retinal Schiff base (RSB) with absorption maximum at 380 nm. Storage of Archon2 at room temperature and refrigerator temperature caused absorption coefficient decrease because of partial protein clustering to aggregates at condensation nuclei and sedimentation. At room temperature an onset of light scattering was observed after two days because of the beginning of protein unfolding. During the period of observation (18 days at 21 °C, 22 days at 3 °C) no change of retinal isomer composition was observed indicating a high potential energy barrier of S0 ground-state isomerization.
    Content: Peer Reviewed
    In: International journal of molecular sciences, Basel : Molecular Diversity Preservation International, 21,2020,18
    Language: English
    URL: Volltext  (kostenfrei)
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