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Article

Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.

Journal of the American Chemical Society - 23 Feb 2022

Najbauer Eszter E, Tekwani Movellan Kumar, Giller Karin, Benz Roland, Becker Stefan, Griesinger Christian, Andreas Loren B

Abstract excerpt

The voltage-dependent anion channel (VDAC), the most abundant protein in the outer mitochondrial membrane, is responsible for the transport of all ions and metabolites into and out of mitochondria. Larger than any of the β-barrel structures determined to date by magic-angle spinning (MAS) NMR, but smaller than the size limit of cryo-electron microscopy (cryo-EM), VDAC1's 31 kDa size has long been a bottleneck in...

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Identifiers

PMID: 35164499
DOI: 10.1021/jacs.1c09848
PMCID: PMC8874904

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.PMID 35164499Read ↗

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