Membrane proteins present a challenge for structural biology. In this article, we review some
of the recent developments that advance the application of NMR to membrane proteins, with …

Membrane proteins have always presented technical challenges for structural studies
because of their requirement for a lipid environment. Multiple approaches exist including X …

The native environment for a membrane protein is a phospholipid bilayer. Because the
protein is immobilized on NMR timescales by the interactions within a bilayer membrane …

Isotopic labeling of methyl-substituted proteinogenic amino acids with 13C has transformed
applications of solution-based NMR spectroscopy and allowed the study of much larger and …

Solid-state NMR spectroscopy (ssNMR) provides increasing possibilities to examine
membrane proteins in different molecular settings, ranging from synthetic bilayers to whole …

The two principal components of biological membranes, the lipid bilayer and the proteins
integrated within it, have coevolved for specific functions that mediate the interactions of …

Rhodopsin is a classical two-state G protein-coupled receptor (GPCR). In the dark, its 11-cis
retinal chromophore serves as an inverse agonist to lock the receptor in an inactive state …

Conserved prolines in the transmembrane helices of G-protein-coupled receptors (GPCRs)
are often considered to function as hinges that divide the helix into two segments capable of …

Most biological functions are carried out in supramolecular assemblies. As a result of their
slow reorientation in solution, these assemblies have been resistant to the widely employed …

Nature has evolved sophisticated mechanisms of producing biomolecular structures that
compartmentalize various biochemical and cellular environments. Biological membranes …