Solid-state NMR, electrophysiology and molecular dynamics characterization of human VDAC2.
J Biomol NMR
; 61(3-4): 311-20, 2015 Apr.
Article
en 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
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Resonancia Magnética Nuclear Biomolecular
/
Canal Aniónico 1 Dependiente del Voltaje
/
Canal Aniónico 2 Dependiente del Voltaje
/
Fenómenos Electrofisiológicos
Límite:
Humans
Idioma:
En
Revista:
J Biomol NMR
Asunto de la revista:
BIOLOGIA MOLECULAR
/
DIAGNOSTICO POR IMAGEM
/
MEDICINA NUCLEAR
Año:
2015
Tipo del documento:
Article
País de afiliación:
Alemania