Abstract

The cellular membrane, a 30-A hydrophobic film, and its molecular components play a central role in both structure and function in the biological world. Solid-state NMR (SSNMR) is a spectroscopic method that is ideally suited to study structure and dynamics of membrane-associated systems. Methodological progress in magic angle spinning (MAS) SSNMR on peptides and proteins has created novel possibilities to examine liposomes and, in particular, membrane proteins (MPs) in a natural lipid environment. Here, we introduce preparatory and experimental aspects of SSNMR on MPs. Furthermore, we consider methodological approaches that deliver structural parameters from SSNMR data. Finally, we discuss recent SSNMR results obtained on MPs and MP complexes containing several hundred amino acids in a lipid bilayer setting. Keywords: GPCR; enzyme; ion channel; histidine kinase; MAS; membrane; membrane protein; solid-state NMR

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