Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2 - Couverture souple

Hey, Melanie

9783954046355: Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

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ISBN 10 : 3954046350 ISBN 13 : 9783954046355

Editeur : Cuvillier, 2014

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�diteur: Cuvillier
Date d'�dition: 2014
Langue: anglais
ISBN 10: 3954046350
ISBN 13: 9783954046355
Reliure: Broch�
Nombre de pages: 234
Coordonn�es du fabricant: info@cuvillier.de
info@cuvillier.de

Nonnenstieg 8
G�ttingen
37075
Allemagne

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Hey, Melanie

Edit� par Cuvillier, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Hey, Melanie

Edit� par Cuvillier, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Melanie Hey

Edit� par Cuvillier Feb 2014, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

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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. N� de r�f. du vendeur 9783954046355

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Hey, Melanie

Edit� par Cuvillier Verlag, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

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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. N� de r�f. du vendeur 68826026

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Melanie Hey

Edit� par Cuvillier Feb 2014, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

Neuf Taschenbuch

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Vendeur : buchversandmimpf2000, Emtmannsberg, BAYE, Allemagne

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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. N� de r�f. du vendeur 9783954046355

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Spectroscopic Studies of Structure and Function of the Light-Gated Cation Channel Channelrhodopsin-2

Melanie Hey

Edit� par Cuvillier, 2014

ISBN 10 : 3954046350 ISBN 13 : 9783954046355

Neuf Taschenbuch

impression � la demande

Vendeur : AHA-BUCH GmbH, Einbeck, Allemagne

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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. N� de r�f. du vendeur 9783954046355

Contacter le vendeur