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5 File Sharing Dangers by the Corliss Group Tech Review

5 File Sharing Dangers by the Corliss Group Tech Review

Sharing files with colleagues and clients should be easy and convenient. What it shouldn't be is a security r…

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The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating

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By Giuseppe Amodeo, Sruthi Murlidaran, Raphael Böhm, Shashank Chavali
| Cell Press Verified
Highlights • β-NADH binding to hVDAC-1 does not change conformation of N-terminal helices • β-NADH binding leads to low VDAC conductance by sterically blocking anion flux • Elevated dynamics of the N-terminal helices are present in the ground state • Movements of helix α2 are important for VDAC gating Summary The voltage-dependent anion channel (VDAC) forms the primary diffusion pore of the outer mitochondrial membrane. In its apo form, VDAC adopts an open conformation with high conductance.
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