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

Gattin, Z.; Schneider, R.; Laukat, Y.; Giller, K.; Maier, E.; Zweckstetter, M.; Griesinger, C.; Benz, R.; Becker, S.; Lange, A.

doi:10.1007/s10858-014-9876-5

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

MPG-Autoren

/persons/resource/persons36441

Gattin, Z.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15783

Schneider, R.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons136193

Laukat, Y.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons36496

Giller, K.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons16093

Zweckstetter, M.
Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15147

Griesinger, C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons14824

Becker, S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15414

Lange, A.
Research Group of Solid-state NMR, MPI for biophysical chemistry, Max Planck Society;

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Zitation

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.

Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0026-C848-A

Zusammenfassung

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.