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Tuning membrane protein mobility by confinement into nanodomains

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

in 631/61/350/1056 / 631/61/350/2093 / 639/925/350/1056 / Binding / Channels / Crystals / Electrons / Escherichia coli - chemistry / Escherichia coli - genetics / Escherichia coli Proteins - chemistry / Escherichia coli Proteins - genetics / Imaging / Lipid Bilayers - chemistry / Lipids / Materials Science / Membrane Proteins - chemistry / Membranes / Microscopy / Microscopy, Atomic Force - methods / Nanostructure / Nanotechnology / Nanotechnology and Microengineering / Protein Domains / Protein Transport / Proteins / Translocation / Tuning

2017

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2017

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2017

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Journal Article

Tuning membrane protein mobility by confinement into nanodomains

Knyazev, Denis G.,

Nimmervoll, Benedikt,

Klotzsch, Enrico,

Winkler, Klemens,

Ollinger, Nicole,

Preiner, Johannes,

Winter, Lukas,

Pohl, Peter,

Plochberger, Birgit,

Siligan, Christine,

Karner, Andreas,

Horner, Andreas,

Kuttner, Roland

2017

Overview

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. Streptavidin crystals grown on mica-supported lipid bilayers can be used as a platform to tune the lateral mobility of transmembrane proteins, allowing the conformation or docking of spatially confined proteins to be imaged with high-speed atomic force microscopy.

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Nature Publishing Group UK,Nature Publishing Group

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