Beriashvili, David, Raymond D. Schellevis, Federico Napoli, Markus Weingarth, and Marc Baldus. “High-Resolution Studies of Proteins in Natural Membranes by Solid-State NMR.” JoVE (Journal of Visualized Experiments), no. 169 (March 3, 2021): e62197.
https://doi.org/10.3791/62197.
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.