Abstract
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-(1 H)-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.
| Original language | English |
|---|---|
| Article number | e62197 |
| Pages (from-to) | 1-22 |
| Number of pages | 22 |
| Journal | Journal of Visualized Experiments |
| Volume | 2021 |
| Issue number | 169 |
| DOIs | |
| Publication status | Published - 3 Mar 2021 |
Bibliographical note
Funding Information:This work is part of the research programs ECHO, TOP, TOP-PUNT, VICI, and VIDI with project numbers 723.014.003, 711.018.001, 700.26.121, 700.10.443, and 718.015.00, which are financed by the Dutch Research Council (NWO).
Publisher Copyright:
© 2021 JoVE Journal of Visualized Experiments.
Funding
This work is part of the research programs ECHO, TOP, TOP-PUNT, VICI, and VIDI with project numbers 723.014.003, 711.018.001, 700.26.121, 700.10.443, and 718.015.00, which are financed by the Dutch Research Council (NWO).