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.
©2011 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques
Articles in the same Issue
- Publisher’s Note
- Publisher’s Note
- Guest Editorial
- Highlight: Membrane transport in light of structure, function, and evolution
- HIGHLIGHT: MEMBRANE TRANSPORT IN LIGHT OF STRUCTURE, FUNCTION, AND EVOLUTION
- Pathways of transport protein evolution: recent advances
- Evolution of YidC/Oxa1/Alb3 insertases: three independent gene duplications followed by functional specialization in bacteria, mitochondria and chloroplasts
- Omp85 in eukaryotic systems: one protein family with distinct functions
- Evolution of ABC transporters by gene duplication and their role in human disease
- A structural and functional analysis of type III periplasmic and substrate binding proteins: their role in bacterial siderophore and heme transport
- The multidrug transporter Pdr5: a molecular diode?
- The lysosomal polypeptide transporter TAPL: more than a housekeeping factor?
- Pumping lipids with P4-ATPases
- Transporters, Trojan horses and therapeutics: suitability of bile acid and peptide transporters for drug delivery
- Substrate recognition and translocation by polyspecific organic cation transporters
- The ugly side of amphetamines: short- and long-term toxicity of 3,4-methylenedioxymethamphetamine (MDMA, ‘Ecstasy’), methamphetamine and d-amphetamine
- SLC22 transporter family proteins as targets for cytostatic uptake into tumor cells
- Role of the Ca2+-activated Cl- channels bestrophin and anoctamin in epithelial cells
- Single-molecule fluorescence resonance energy transfer techniques on rotary ATP synthases
- Structure determination of channel and transport proteins by high-resolution microscopy techniques