Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.
J Biomol NMR
; 61(3-4): 311-20, 2015 Apr.
Article
em En
| MEDLINE
| ID: mdl-25399320
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Ressonância Magnética Nuclear Biomolecular
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Canal de Ânion 1 Dependente de Voltagem
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Canal de Ânion 2 Dependente de Voltagem
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Fenômenos Eletrofisiológicos
Limite:
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article