ArticleNature nanotechnology2017
Tuning membrane protein mobility by confinement into nanodomains.
Article in Nature nanotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Visualizing the Functional Dynamics of P-Glycoprotein and Its Modulation by Elacridar via High-Speed Atomic Force Microscopy.International journal of molecular sciences · 2025Article
- AFM observation of protein translocation mediated by one unit of SecYEG-SecA complex.Nature communications · 2025Article
- Complement activation by IgG subclasses is governed by their ability to oligomerize upon antigen binding.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022Article
- CRISPR/Cas9 Genome Editing vs. Over-Expression for Fluorescent Extracellular Vesicle-Labeling: A Quantitative Analysis.International journal of molecular sciences · 2021Article
- ScatteringNanoscale advances · 2021Article
- Label-free characterization of an extracellular vesicle-based therapeutic.Journal of extracellular vesicles · 2021Article
- DNA origami demonstrate the unique stimulatory power of single pMHCs as T cell antigens.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Protein Translocation Activity in Surface-Supported Lipid Bilayers.Langmuir : the ACS journal of surfaces and colloids · 2019Article
- Localized detection of ions and biomolecules with a force-controlled scanning nanopore microscope.Nature nanotechnology · 2019Article
- Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters.Current opinion in structural biology · 2019Review
- Article
- High-speed AFM height spectroscopy reveals µs-dynamics of unlabeled biomolecules.Nature communications · 2018Article
- Single-file transport of water through membrane channels.Faraday discussions · 2018Article
- Spatially confined lignin nanospheres for biocatalytic ester synthesis in aqueous media.Nature communications · 2018Article
- Quantification of Water Flux in Vesicular Systems.Scientific reports · 2018Article
- HDL particles incorporate into lipid bilayers - a combined AFM and single molecule fluorescence microscopy study.Scientific reports · 2017Article
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Authors and funding
13 authors.
Funding
Abstract
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, non-interacting membrane supports and by high protein mobility. Here we show that streptavidin crystals grown on mica-supported 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.
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