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Structure determination of channel and transport proteins by high-resolution microscopy techniques

  • Marcel Meury , Daniel Harder , Zöhre Ucurum , Rajendra Boggavarapu , Jean-Marc Jeckelmann and Dimitrios Fotiadis EMAIL logo
Published/Copyright: June 18, 2011
Biological Chemistry
From the journal Volume 392 Issue 1-2

Abstract

High-resolution microscopy techniques provide a plethora of information on biological structures from the cellular level down to the molecular level. In this review, we present the unique capabilities of transmission electron and atomic force microscopy to assess the structure, oligomeric state, function and dynamics of channel and transport proteins in their native environment, the lipid bilayer. Most importantly, membrane proteins can be visualized in the frozen-hydrated state and in buffer solution by cryo-transmission electron and atomic force microscopy, respectively. We also illustrate the potential of the scintillation proximity assay to study substrate binding of detergent-solubilized transporters prior to crystallization and structural characterization.


Corresponding author

Received: 2010-8-31
Accepted: 2010-9-16
Published Online: 2011-06-18
Published in Print: 2011-02-01

©2011 by Walter de Gruyter Berlin New York

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  1. Publisher’s Note
  2. Publisher’s Note
  3. Guest Editorial
  4. Highlight: Membrane transport in light of structure, function, and evolution
  5. HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
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  18. Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
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  20. Structure determination of channel and transport proteins by high-resolution microscopy techniques
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