Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT
Zur Ablage hinzufügen
  DetailsÜbersicht

Freigegeben
Zeitschriftenartikel

Spatial distribution and activity of Na +/K +-ATPase in lipid bilayer membranes with phase boundaries

MPG-Autoren
/persons/resource/persons191852

Bhatia,  Tripta
Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

Externe Ressourcen
Es sind keine externen Ressourcen hinterlegt
Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Bhatia, T., Cornelius, F., Brewer, J., Bagatolli, L. A., Simonsen, A. C., Ipsen, J. H., et al. (2016). Spatial distribution and activity of Na +/K +-ATPase in lipid bilayer membranes with phase boundaries. Biochimica et Biophysica Acta (BBA) - Biomembranes, 1858(6), 1390-1399. doi:10.1016/j.bbamem.2016.03.015.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002A-22B4-A
Zusammenfassung
Abstract We have reconstituted functional Na +/K +-ATPase (NKA) into giant unilamellar vesicles (GUVs) of well-defined binary and ternary lipid composition including cholesterol. The activity of the membrane system can be turned on and off by ATP. The hydrolytic activity of \NKA\} is found to depend on membrane phase, and the water relaxation in the membrane on the presence of NKA. By collapsing and fixating the \{GUVs\} onto a solid support and using high-resolution atomic-force microscopy (AFM) imaging we determine the protein orientation and spatial distribution at the single-molecule level and find that \{NKA\} is preferentially located at l o/l d interfaces in two-phase \{GUVs\ and homogeneously distributed in single-phase GUVs. When turned active, the membrane is found to unbind from the support suggesting that the protein function leads to a softening of the membrane.