• Port-a-Patch

    世界最小パッチクランプセットアップ
  • Port-a-Patch

    誰でもデータ取得 - 教育ツールとして最適
  • Port-a-Patch

    細胞, オルガネラ, 脂質二分子膜
  • Port-a-Patch

    世界で最も歴史あるプレーナー式パッチクランプ装置
  • Port-a-Patch

    細胞内灌流実験に最適

2021 - Structure, gating and interactions of the voltage-dependent anion channel

icon pap  Port-a-Patch Publication in European Biophysics Journal (2021)

Authors:
Najbauer E.E., Becker S., Giller K., Zweckstetter M., Lange A., Steinem C., de Groot B.L., Griesinger C., Andreas L.B.

Journal: 
European Biophysics Journal (2021) doi: 10.1007/s00249-021-01515-7


Abstract: 

The voltage-dependent anion channel (VDAC) is one of the most highly abundant proteins found in the outer mitochondrial membrane, and was one of the earliest discovered. Here we review progress in understanding VDAC function with a focus on its structure, discussing various models proposed for voltage gating as well as potential drug targets to modulate the channel’s function. In addition, we explore the sensitivity of VDAC structure to variations in the membrane environment, comparing DMPC-only, DMPC with cholesterol, and near-native lipid compositions, and use magic-angle spinning NMR spectroscopy to locate cholesterol on the outside of the β-barrel. We find that the VDAC protein structure remains unchanged in different membrane compositions, including conditions with cholesterol.


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