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Ernst Bamberg

Biophysiker

Name	Ernst Bamberg
Time	1971- (Wirkungsdaten)
Place	Frankfurt am Main (Wirkungsort) Deutschland
Gender	männlich
Academic degree	Prof. Dr. phil.
Profession	Biophysiker (characteristic profession)
Related	Max-Planck-Institut für Biophysik
Further information	Fachgebiet: Biophysik
Record type	Person
GND-Identifier	1020424516
Record ID	1020424516
Involved in show all The Voltage Dependent Sidedness of the Reprotonation of the Retinal Schiff Base Determines the Unique Inward Pumping of Xenorhodopsin Electrophysiological analysis of the mutated Na,K-ATPase cation binding pocket Fluorometric measurements of intermolecular distances between the α- and β-Subunits of the Na+/K+-ATPase Functional significance of E2 state stabilization by specific α/β-subunit interactions of Na,K- and H,K-ATPase The voltage dependent sidedness of the reprotonation of the retinal schiff base determines the unique inward pumping of xenorhodopsin The voltage dependent sidedness of the reprotonation of the retinal schiff base determines the unique inward pumping of xenorhodopsin Functional maturation of human stem cell-derived neurons in long-term cultures Licht steuert Nervenzellen mit höchster Präzision : Die Optogenetik revolutioniert die Neurowissenschaften Light-induced helix movements in channelrhodopsin-2 Voltage dependence of proton pumping by bacteriorhodopsin mutants with altered lifetime of the m intermediate Sucrose- and H+-dependent charge movements associated with the gating of sucrose transporter ZmSUT1 Effects of Electrical Charges on the Permeability of the Gramicidin Channel Effects of Surface Charge on the Conductance of the Gramicidin Channel Formation of ion channels by a negatively charged analog of Gramicidin A Gramicidin channel controversy the structure in a lipid environment Kinetics of Na+-dependent conformational changes of rabbit kidney Na+,K+-ATPase The sodium pump : structure mechanism, hormonal control and its role in disease Elektrochemische Untersuchungen an bimolekularen Lipidmembranen in Gegenwart von Entkopplern der oxidativen Phosphorylierung

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Ernst Bamberg

The Voltage Dependent Sidedness of the Reprotonation of the Retinal Schiff Base Determines the Unique Inward Pumping of Xenorhodopsin

Electrophysiological analysis of the mutated Na,K-ATPase cation binding pocket

Fluorometric measurements of intermolecular distances between the α- and β-Subunits of the Na+/K+-ATPase

Functional significance of E2 state stabilization by specific α/β-subunit interactions of Na,K- and H,K-ATPase

The voltage dependent sidedness of the reprotonation of the retinal schiff base determines the unique inward pumping of xenorhodopsin

The voltage dependent sidedness of the reprotonation of the retinal schiff base determines the unique inward pumping of xenorhodopsin

Functional maturation of human stem cell-derived neurons in long-term cultures

Licht steuert Nervenzellen mit höchster Präzision : Die Optogenetik revolutioniert die Neurowissenschaften

Light-induced helix movements in channelrhodopsin-2

Voltage dependence of proton pumping by bacteriorhodopsin mutants with altered lifetime of the m intermediate

Sucrose- and H+-dependent charge movements associated with the gating of sucrose transporter ZmSUT1

Effects of Electrical Charges on the Permeability of the Gramicidin Channel

Effects of Surface Charge on the Conductance of the Gramicidin Channel

Formation of ion channels by a negatively charged analog of Gramicidin A

Gramicidin channel controversy the structure in a lipid environment

Kinetics of Na+-dependent conformational changes of rabbit kidney Na+,K+-ATPase

The sodium pump : structure mechanism, hormonal control and its role in disease

Elektrochemische Untersuchungen an bimolekularen Lipidmembranen in Gegenwart von Entkopplern der oxidativen Phosphorylierung