Tuning membrane protein mobility by confinement into nanodomains

Andreas Karner, Benedikt Nimmervoll, Birgit Plochberger, Enrico Klotzsch, Andreas Horner, Denis Knyazev, Roland Kuttner, Klemens Winkler, Lukas Winter, Christine Siligan, Nicole Ollinger, Peter Pohl, Johannes Preiner

Research output: Contribution to journalArticlepeer-review

32 Citations (Scopus)


High-speed atomic force microscopy (HS-AFM) can be used to visualize function-related conformational changes of single soluble proteins. Similar studies of single membrane proteins are, however, hampered by a lack of suitable flat, noninteracting membrane supports and by high protein mobility. Here we show that streptavidin crystals grown on micasupported lipid bilayers can be used as porous supports for membranes containing biotinylated lipids. Using SecYEG (protein translocation channel) and GlpF (aquaglyceroporin), we demonstrate that the platform can be used to tune the lateral mobility of transmembrane proteins to any value within the dynamic range accessible to HS-AFM imaging through glutaraldehyde-cross-linking of the streptavidin. This allows HS-AFM to study the conformation or docking of spatially confined proteins, which we illustrate by imaging GlpF at sub-molecular resolution and by observing the motor protein SecA binding to SecYEG.
Original languageEnglish
Pages (from-to)260-266
Number of pages7
JournalNature Nanotechnology
Issue number3
Publication statusPublished - 7 Mar 2017


  • Escherichia coli/chemistry
  • Escherichia coli Proteins/chemistry
  • Lipid Bilayers/chemistry
  • Membrane Proteins/chemistry
  • Microscopy, Atomic Force/methods
  • Protein Domains
  • Protein Transport


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