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

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.

journal_name

J Biomol NMR

authors

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

subject

Has Abstract

pub_date

2015-04-01 00:00:00

pages

311-20

issue

3-4

eissn

0925-2738

issn

1573-5001

journal_volume

61

pub_type

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