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

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.

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 Creators:
Bhatia, Tripta1, Author           
Cornelius, Flemming, Author
Brewer, Jonathan, Author
Bagatolli, Luis A., Author
Simonsen, Adam C., Author
Ipsen, John H., Author
Mouritsen, Ole G., Author
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1Rumiana Dimova, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863328              

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Free keywords: Membranes; Na +/K +-ATPase; Giant Unilamellar Vesicles; Domains; Membrane Protein; Protein-Lipid Interaction; Membrane Biophysics
 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 softening of the membrane.

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 Dates: 2016-03-162016
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.1016/j.bbamem.2016.03.015
BibTex Citekey: Bhatia2016
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Title: Biochimica et Biophysica Acta (BBA) - Biomembranes
  Abbreviation : BBA
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 1858 (6) Sequence Number: - Start / End Page: 1390 - 1399 Identifier: ISSN: 0005-2736