High-resolution studies of proteins in natural membranes by solid-state nmr

David Beriashvili, Raymond D. Schellevis, Federico Napoli, Markus Weingarth*, Marc Baldus

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review


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 languageEnglish
Article numbere62197
Pages (from-to)1-22
Number of pages22
JournalJournal of Visualized Experiments
Issue number169
Publication statusPublished - 3 Mar 2021


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