High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR
| Autor: | David Beriashvili, Marc Baldus, Federico Napoli, Markus Weingarth, Raymond D. Schellevis |
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| Rok vydání: | 2021 |
| Předmět: |
Potassium Channels
Proteolipids General Chemical Engineering KcsA potassium channel Protein Refolding General Biochemistry Genetics and Molecular Biology Bacterial Proteins Point Mutation Nuclear Magnetic Resonance Biomolecular Ion channel Inclusion Bodies Staining and Labeling General Immunology and Microbiology Chemistry General Neuroscience Cell Membrane Membrane Proteins Biological membrane Nuclear magnetic resonance spectroscopy Membrane Solid-state nuclear magnetic resonance Membrane protein Structural biology Isotope Labeling Biophysics Protons |
| Zdroj: | Journal of Visualized Experiments |
| ISSN: | 1940-087X |
| DOI: | 10.3791/62197 |
| Popis: | Membrane proteins are vital for cell function and thus represent important drug targets. Solid-state Nuclear Magnetic Resonance (ssNMR) spectroscopy offers a unique access to probe the structure and dynamics of such proteins in biological membranes of increasing complexity. Here, we present modern solid-state NMR spectroscopy as a tool to study structure and dynamics of proteins in natural lipid membranes and at atomic scale. Such spectroscopic studies profit from the use of high-sensitivity ssNMR methods, i.e., proton-(1H)-detected ssNMR and DNP (Dynamic Nuclear Polarization) supported ssNMR. Using bacterial outer membrane beta-barrel protein BamA and the ion channel KcsA, we present methods to prepare isotope-labeled membrane proteins and to derive structural and motional information by ssNMR. |
| Databáze: | OpenAIRE |
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