The voltage-dependent anion channel (VDAC) mediates trafficking of small molecules and ions across the eukaryotic outer mitochondrial membrane. VDAC also interacts with anti-apoptotic proteins from the Bcl-2 family and this interaction inhibits release of apoptogenic proteins from the mitochondrion. We present the NMR solution structure of recombinant human VDAC-1 reconstituted in detergent micelles. It forms a 19-stranded β-barrel with the first and last strand parallel. The hydrophobic outside perimeter of the barrel is covered by detergent molecules in a belt-like fashion. In the presence of cholesterol recombinant VDAC-1 can form voltage-gated channels in phospholipid bilayers similar to the native protein. NMR measurements revealed the binding sites of VDAC-1 for the Bcl-2 protein Bcl-xL, for β-NADH and for cholesterol. Bcl-xL interacts with the VDAC barrel laterally at strands 17 and 18.

High‐quality multidimensional NMR spectra can be obtained from rapidly recorded non‐uniformly sampled (NUS) data. The inherent loss of the spectrum quality usually associated with NUS data is compensated by compressed sensing (CS); left spectrum: Nyquist–Shannon sampling, 22 h acquisition time, Fourier transform; right: CS non‐linear sampling, 8.5 h acquisition time, Ip norm minimization.

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