Spectroscopic studies structure function par hey melanie (6 résultats)

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  • Langue : anglais

    Edité par Cuvillier, 2014

    3954046350 / 9783954046355

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  • Langue : anglais

    Edité par Cuvillier, 2014

    3954046350 / 9783954046355

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  • Langue : anglais

    Edité par Cuvillier Feb 2014, 2014

    3954046350 / 9783954046355

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    Vendeur : BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, AllemagneBuchWeltWeit Ludwig Meier e.K.

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    Taschenbuch. Etat : Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Revealing structural and mechanistic details of Channelrhodopsin-2 (ChR2) is in the focus of current scientific research due to its unique ability to stimulate cell activity by light (optogenetics). Hence, ChR2 is a promising tool to revolutionize medical treatment. The aim of this work was the investigation of the light-activated mechanism of the retinylidene cation channel ChR2 on an atomistic level by means of vibrational spectroscopy.In addition to successful expression and purification of ChR2, resonance Raman and FTIR spectroscopy elucidated the structure of the chromophore binding pocket as well as the gating mechanism triggered by a single hydrogen bond between two residues ('DC gate'). Therefore, FTIR difference spectroscopic results were correlated with time-resolved UV/Vis spectroscopy. Flash photolysis allowed characterization of the time scale of proton release with subsequent uptake using an indicator dye.Application and modification of advanced biophysical techniques such as surface-enhanced FTIR, single-molecule force spectroscopy and doubly vibrationally-enhanced four wave mixing set the basis to obtain even deeper insights into the structure and function of membrane proteins like ChR2. 234 pp. Englisch. …

  • Langue : anglais

    Edité par Cuvillier Verlag, 2014

    3954046350 / 9783954046355

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    Vendeur : moluna, Greven, Allemagnemoluna

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    Etat : New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. &Uumlber den AutorrnrnMelanie Hey (geb. Nack) hat ihr Diplom-Biochemie-Studium an der Universitaet Bielefeld im Jahr 2008 abgeschlossen. Im direkten Anschluss hat sie ihre Doktorarbeit in der biohysikalischen Chemie der Universitaet Bielefeld beg.…

  • Langue : anglais

    Edité par Cuvillier, 2014

    3954046350 / 9783954046355

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    Vendeur : AHA-BUCH GmbH, Einbeck, AllemagneAHA-BUCH GmbH

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    Taschenbuch. Etat : Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Revealing structural and mechanistic details of Channelrhodopsin-2 (ChR2) is in the focus of current scientific research due to its unique ability to stimulate cell activity by light (optogenetics). Hence, ChR2 is a promising tool to revolutionize medical treatment. The aim of this work was the investigation of the light-activated mechanism of the retinylidene cation channel ChR2 on an atomistic level by means of vibrational spectroscopy.In addition to successful expression and purification of ChR2, resonance Raman and FTIR spectroscopy elucidated the structure of the chromophore binding pocket as well as the gating mechanism triggered by a single hydrogen bond between two residues ('DC gate'). Therefore, FTIR difference spectroscopic results were correlated with time-resolved UV/Vis spectroscopy. Flash photolysis allowed characterization of the time scale of proton release with subsequent uptake using an indicator dye.Application and modification of advanced biophysical techniques such as surface-enhanced FTIR, single-molecule force spectroscopy and doubly vibrationally-enhanced four wave mixing set the basis to obtain even deeper insights into the structure and function of membrane proteins like ChR2.…

  • Langue : anglais

    Edité par Cuvillier Feb 2014, 2014

    3954046350 / 9783954046355

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    Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagnebuchversandmimpf2000

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    Taschenbuch. Etat : Neu. This item is printed on demand - Print on Demand Titel. Neuware -Revealing structural and mechanistic details of Channelrhodopsin-2 (ChR2) is in the focus of current scientific research due to its unique ability to stimulate cell activity by light (optogenetics). Hence, ChR2 is a promising tool to revolutionize medical treatment. The aim of this work was the investigation of the light-activated mechanism of the retinylidene cation channel ChR2 on an atomistic level by means of vibrational spectroscopy.In addition to successful expression and purification of ChR2, resonance Raman and FTIR spectroscopy elucidated the structure of the chromophore binding pocket as well as the gating mechanism triggered by a single hydrogen bond between two residues ('DC gate'). Therefore, FTIR difference spectroscopic results were correlated with time-resolved UV/Vis spectroscopy. Flash photolysis allowed characterization of the time scale of proton release with subsequent uptake using an indicator dye.Application and modification of advanced biophysical techniques such as surface-enhanced FTIR, single-molecule force spectroscopy and doubly vibrationally-enhanced four wave mixing set the basis to obtain even deeper insights into the structure and function of membrane proteins like ChR2. 234 pp. Englisch.…