High resolution structure and double electron-electron resonance of the zebrafish voltage-dependent anion channel 2 reveal an oligomeric population.

Schredelseker, Johann; Paz, Aviv; López, Carlos J; Altenbach, Christian; Leung, Calvin S; Drexler, Maria K; Chen, Jau-Nian; Hubbell, Wayne L; Abramson, Jeff

Schredelseker, Johann; Paz, Aviv; López, Carlos J; Altenbach, Christian; Leung, Calvin S; Drexler, Maria K; Chen, Jau-Nian; Hubbell, Wayne L; Abramson, Jeff.

Affiliation

Schredelseker J; From the Department of Molecular, Cell and Developmental Biology.

J Biol Chem ; 289(18): 12566-77, 2014 May 02.

Article in En | MEDLINE | ID: mdl-24627492

Subject(s)

Electron Spin Resonance Spectroscopy/methods; Protein Multimerization; Voltage-Dependent Anion Channel 2/chemistry; Zebrafish Proteins/chemistry; Amino Acid Sequence; Animals; Crystallography, X-Ray; Cysteine/chemistry; Cysteine/genetics; Cysteine/metabolism; Electric Conductivity; Electrophoresis, Polyacrylamide Gel; Lipid Bilayers/chemistry; Models, Molecular; Molecular Sequence Data; Mutation; Protein Conformation; Protein Structure, Secondary; Sequence Homology, Amino Acid; Static Electricity; Voltage-Dependent Anion Channel 2/genetics; Voltage-Dependent Anion Channel 2/metabolism; Zebrafish Proteins/genetics; Zebrafish Proteins/metabolism

Key words

Biophysics; DEER; Ion Channels; Mitochondria; VDAC2; X-ray Crystallography; Zebrafish

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Electron Spin Resonance Spectroscopy / Zebrafish Proteins / Voltage-Dependent Anion Channel 2 / Protein Multimerization Limits: Animals Language: En Journal: J Biol Chem Year: 2014 Type: Article

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