Membrane proteins are highly diverse in both structure and function and can, therefore,
present different challenges for structure determination. They are biologically important for …

Membrane proteins (MPs) play essential roles in numerous cellular processes. Because
around 70% of the currently marketed drugs target MPs, a detailed understanding of their …

Membrane proteins are a highly relevant class of biological molecules and comprise∼ 60%
of current drug targets. Before being analyzed by structural, biochemical, and biophysical …

Atomic-resolution structural studies of membrane-associated proteins and peptides in a
membrane environment are important to fully understand their biological function and the …

Abstract Phe-Met-Arg-Phe-amide (FMRFamide)-activated sodium channels (FaNaCs) are a
family of channels activated by the neuropeptide FMRFamide, and, to date, the underlying …

Acid-sensing ion channels (ASICs) are proton-gated cation channels that are involved in
diverse neuronal processes including pain sensing. The peptide toxin Mambalgin1 …

The advent of amphiphilic copolymers enables integral membrane proteins to be solubilized
into stable 10–30 nm native nanodiscs to resolve their multisubunit structures, post …

Epithelial sodium channels (ENaC) are part of a complex network of interacting biochemical
pathways and as such are involved in several disease states. Dependent on site and type of …

The solubilisation of membrane proteins (MPs) necessitates the overlap of two contradictory
events; the extraction of MPs from their native lipid membranes and their subsequent …

The molecular bases of heteromeric assembly and link between Na+ self-inhibition and
protease-sensitivity in epithelial sodium channels (ENaCs) are not fully understood …