Tuning membrane protein mobility by confinement into nanodomains View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-03

AUTHORS

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

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. More... »

PAGES

260-266

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nnano.2016.236

    DOI

    http://dx.doi.org/10.1038/nnano.2016.236

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1020979010

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/27842062


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