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

Meury, Marcel ; Harder, Daniel ; Ucurum, Zöhre ; Boggavarapu, Rajendra ; Jeckelmann, Jean-Marc ; Fotiadis, Dimitrios

In: Biological Chemistry, 2011, vol. 392, no. 1-2, p. 143-150

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    Titre
    • Structure determination of channel and transport proteins by high-resolution microscopy techniques
    Auteur
    • Meury, Marcel. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    • Harder, Daniel. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    • Ucurum, Zöhre. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    • Boggavarapu, Rajendra. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    • Jeckelmann, Jean-Marc. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    • Fotiadis, Dimitrios. Institute of Biochemistry and Molecular Medicine, and NCCR TransCure, University of Bern, Bühlstrasse 28, CH-3012 Bern, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Biological Chemistry, 2011, vol. 392, no. 1-2, p. 143-150. Walter de Gruyter
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:294163
    Summary
    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