Flexibility of the N-terminal mVDAC1 segment controls the channel's gating behavior

Since the solution of the molecular structures of members of the voltage dependent anion channels (VDACs), the N-terminal α-helix has been the main focus of attention, since its strategic location, in combination with its putative conformational flexibility, could define or control the channel'...

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Veröffentlicht in:	PloS one 2012-10, Vol.7 (10), p.e47938
Hauptverfasser:	Mertins, Barbara, Psakis, Georgios, Grosse, Wolfgang, Back, Katrin Christiane, Salisowski, Anastasia, Reiss, Philipp, Koert, Ulrich, Essen, Lars-Oliver
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Anion channels Bioenergetics Biology Channel gating Chemistry Cloning, Molecular Crosslinking Cysteine DNA Primers - genetics Electrophoresis, Polyacrylamide Gel Engineering Flexibility Genetic Engineering Hypotheses Inclusion Bodies - metabolism Ion Channel Gating - genetics Ion Channel Gating - physiology Lipid membranes Lipids Mice Models, Molecular Mutagenesis Mutagenesis, Site-Directed Mutation Oxidation-Reduction Protein Conformation Protein Folding Proteins Voltage-Dependent Anion Channel 1 - chemistry Voltage-Dependent Anion Channel 1 - genetics Voltage-Dependent Anion Channel 1 - metabolism
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