Details

Autor(en) / Beteiligte

• Gattin, Zrinka
• Schneider, Robert
• Laukat, Yvonne
• Giller, Karin
• Maier, Elke
• Zweckstetter, Markus
• Griesinger, Christian
• Benz, Roland
• Becker, Stefan
• Lange, Adam

Titel

Solid-state NMR and Molecular Dynamics Characterization of human VDAC2

Ist Teil von

• Journal of biomolecular NMR, 2014-11, Vol.61 (3-4), p.311-320

Erscheinungsjahr

2014

Link zum Volltext

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• 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 plasticity compared to hVDAC1 which is reflected in broader solid-state NMR spectra and less defined electrophysiological profiles.