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  Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.

Gattin, Z., Schneider, R., Laukat, Y., Giller, K., Maier, E., Zweckstetter, M., et al. (2015). Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2. Journal of Biomolecular NMR, 61(3-4), 311-320. doi:10.1007/s10858-014-9876-5.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0026-C848-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-58FC-2
Genre: Journal Article

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2151827.pdf (Publisher version), 3MB
 
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 Creators:
Gattin, Z.1, Author              
Schneider, R.2, Author              
Laukat, Y.2, Author              
Giller, K.2, Author              
Maier, E., Author
Zweckstetter, M.3, Author              
Griesinger, C.2, Author              
Benz, R., Author
Becker, S.2, Author              
Lange, A.1, Author              
Affiliations:
1Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society, ou_persistent35              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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Free keywords: Voltage-dependent anion channel; Membrane proteins; Solid-state NMR; Molecular dynamics simulations
 Abstract: 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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Language(s): eng - English
 Dates: 2014-11-162015-04
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s10858-014-9876-5
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Title: Journal of Biomolecular NMR
Source Genre: Journal
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Pages: - Volume / Issue: 61 (3-4) Sequence Number: - Start / End Page: 311 - 320 Identifier: -