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Reviews in Analytical Chemistry

Editor-in-Chief: Schechter, Israel

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Volume 33, Issue 3


Chromatographic and electrophoretic methods for nanodisc purification and analysis

Bo Højen Justesen
  • Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Thomas Günther-Pomorski
  • Corresponding author
  • Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark
  • Email
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2014-08-28 | DOI: https://doi.org/10.1515/revac-2014-0014


Soluble nanoscale lipid bilayers, termed nanodiscs, are widely used in science for studying the membrane-anchored and integral membrane protein complexes under defined experimental conditions. Although their formation occurs by a self-assembly process, nanodisc purification and the verification of proper reconstitution are still major challenges during the sample preparation. This review gives an overview of the methods used for purifying and analyzing nanodiscs and nanodisc-reconstituted membrane proteins, with an emphasis on the chromatographic and electrophoretic approaches.

This article offers supplementary material which is provided at the end of the article.

Keywords: chromatography; free flow electrophoresis; mass spectrometry; nanodiscs; native PAGE


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About the article

Bo Højen Justesen

Bo Justesen received his Master of Science Degree in Engineering, Nano- and Biotechnology from the University of Aalborg in 2008. In 2013 he completed his PhD studies in Biotechnology at the University of Copenhagen. His thesis work focused on the reconstitution of a plant plasma membrane proton ATPase into nanodiscs for structural and functional characterization. His postdoctoral work involves the application of nanodisc and styrene maleic acid lipid particle (SMALP) technologies to study functional membrane proteins.

Thomas Günther-Pomorski

Thomas Günther-Pomorski studied Biophysics at the Humboldt University of Berlin, where he received his PhD in 1996. After postdoctoral research experience at the Max Planck Institute for Infection Biology in Berlin, the Academic Medical Center in Amsterdam and the Utrecht University, The Netherlands, he became a Junior Professor for Cell Biophysics at the Humboldt University of Berlin, Germany. In 2009 he was appointed as Associate Professor of Membrane Biology at University of Copenhagen. His lab currently develops and applies biophysical methods to study organization, function and regulation of membrane pumps.

Corresponding author: Thomas Günther-Pomorski, Department of Plant and Environmental Sciences, University of Copenhagen, Thorvaldsensvej 40, DK-1871 Frederiksberg C, Denmark, e-mail:

Received: 2014-05-01

Accepted: 2014-08-01

Published Online: 2014-08-28

Published in Print: 2014-10-01

Citation Information: Reviews in Analytical Chemistry, Volume 33, Issue 3, Pages 165–172, ISSN (Online) 2191-0189, ISSN (Print) 0793-0135, DOI: https://doi.org/10.1515/revac-2014-0014.

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