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  Molecular plasticity of the human Voltage-Dependent Anion Channel embedded into a membrane.

Ge, L., Villinger, S., Mari, S. A., Giller, K., Griesinger, C., Becker, S., et al. (2016). Molecular plasticity of the human Voltage-Dependent Anion Channel embedded into a membrane. Structure, 24(4), 585-594. doi:10.1016/j.str.2016.02.012.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5768-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-AC77-4
Genre: Journal Article

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 Creators:
Ge, L., Author
Villinger, S.1, Author              
Mari, S. A., Author
Giller, K.2, Author              
Griesinger, C.2, Author              
Becker, S.2, Author              
Müller, D. J., Author
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: The voltage-dependent anion channel (VDAC) regulates the flux of metabolites and ions across the outer mitochondrial membrane. Regulation of ion flow involves conformational transitions in VDAC, but the nature of these changes has not been resolved to date. By combining single-molecule force spectroscopy with nuclear magnetic resonance spectroscopy we show that the β barrel of human VDAC embedded into a membrane is highly flexible. Its mechanical flexibility exceeds by up to one order of magnitude that determined for β strands of other membrane proteins and is largest in the N-terminal part of the β barrel. Interaction with Ca2+, a key regulator of metabolism and apoptosis, considerably decreases the barrel's conformational variability and kinetic free energy in the membrane. The combined data suggest that physiological VDAC function depends on the molecular plasticity of its channel.

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Language(s): eng - English
 Dates: 2016-03-242016-04-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.str.2016.02.012
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Title: Structure
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Pages: - Volume / Issue: 24 (4) Sequence Number: - Start / End Page: 585 - 594 Identifier: -