Journal
BIOLOGICAL CHEMISTRY
Volume 392, Issue 1-2, Pages 143-150Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/BC.2011.004
Keywords
atomic force microscopy; electron crystallography; membrane protein; scintillation proximity assay; transmission electron microscopy; transporter; two-dimensional crystal
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Funding
- Swiss National Foundation for Scientific Research [31003A_125150]
- Bern University Research Foundation
- Novartis Foundation
- European Science Foundation [09-EuroSYNBIO-FP-012 NANOCELL]
- National Center of Competence in Research (NCCR) TransCure
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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.
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