期刊
JOURNAL OF BIOMOLECULAR NMR
卷 61, 期 3-4, 页码 311-320出版社
SPRINGER
DOI: 10.1007/s10858-014-9876-5
关键词
Voltage-dependent anion channel; Membrane proteins; Solid-state NMR; Molecular dynamics simulations
资金
- Max Planck Society
- Leibniz-Institut fur Molekulare Pharmakologie
- ERC [282008]
- DFG (Collaborative research center 803)
- Emmy Noether Fellowship
- Marie Curie fellowship within the 7th EU Framework Program
- European Research Council (ERC) [282008] Funding Source: European Research Council (ERC)
The voltage-dependent anion channel (VDAC) is the most abundant protein of the outer mitochondrial membrane and constitutes the major pathway for the transport of ADP, ATP, and other metabolites. In this multidisciplinary study we combined solid-state NMR, electrophysiology, and molecular dynamics simulations, to study the structure of the human VDAC isoform 2 in a lipid bilayer environment. We find that the structure of hVDAC2 is similar to the structure of hVDAC1, in line with recent investigations on zfVDAC2. However, hVDAC2 appears to exhibit an increased conformational heterogeneity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles.
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