Hochschulschrift
Voltage dependent anion channel: Interaction with lipid membranes
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Dresden, Technische Universität Dresden, Diss., 2012
- Keyword
-
Membranproteine
Carrier-Proteine
Molekülstruktur
Strukturbiologie
- Event
-
Veröffentlichung
- (where)
-
Dresden
- (who)
-
Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden
- (when)
-
2012
- Event
-
Veröffentlichung
- (where)
-
Dresden
- (who)
-
Technische Universität Dresden
- (when)
-
2012
- Creator
- Contributor
- URN
-
urn:nbn:de:bsz:14-qucosa-85742
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:35 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Object type
- Hochschulschrift
Associated
- Betaneli, Viktoria
- Schwille, Petra
- Eng, Lukas
- Ravens, Ursula
- Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden
- Technische Universität Dresden
Time of origin
- 2012
Other Objects (12)
Voltage dependent anion channel: interaction with lipid membranes
Structure, gating and interactions of the voltage-dependent anion channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I
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Anion carriers of mitochondrial membranes
Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
Dynamics and interactions of the voltage-dependent anion channel 1 studied by NMR spectroscopy
Characterization of voltage dependent anion channel (VDAC) subtypes in mammalian follicles and potential physiological relevance
Lipid protein interactions in lipid membranes
The antimicrobial fibupeptide lugdunin forms water-filled channel structures in lipid membranes
Solvation-Driven Actuation of Anion-Exchange Membranes
Solvation‐Driven Actuation of Anion‐Exchange Membranes
Voltage dependent anion channel: interaction with lipid membranes
Structure, gating and interactions of the voltage-dependent anion channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I
Studien zur Funktionsbestimmung von plasmamembranal exprimiertem VDAC (Voltage dependent Anion selective channel)
Anion carriers of mitochondrial membranes
Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
Dynamics and interactions of the voltage-dependent anion channel 1 studied by NMR spectroscopy
Characterization of voltage dependent anion channel (VDAC) subtypes in mammalian follicles and potential physiological relevance
Lipid protein interactions in lipid membranes
The antimicrobial fibupeptide lugdunin forms water-filled channel structures in lipid membranes
Solvation-Driven Actuation of Anion-Exchange Membranes
Solvation‐Driven Actuation of Anion‐Exchange Membranes
Voltage dependent anion channel: interaction with lipid membranes
Structure, gating and interactions of the voltage-dependent anion channel
Structural basis of the mitochondrial voltage-dependent anion channel VDAC I
Studien zur Funktionsbestimmung von plasmamembranal exprimiertem VDAC (Voltage dependent Anion selective channel)
Anion carriers of mitochondrial membranes
Gating of the voltage-dependent chloride channel ClC-0 by the permeant anion
Dynamics and interactions of the voltage-dependent anion channel 1 studied by NMR spectroscopy
Characterization of voltage dependent anion channel (VDAC) subtypes in mammalian follicles and potential physiological relevance
Lipid protein interactions in lipid membranes
The antimicrobial fibupeptide lugdunin forms water-filled channel structures in lipid membranes
Solvation-Driven Actuation of Anion-Exchange Membranes