Jonas M. Dörr

TL;DR: Current methods of membrane protein solubilization and stabilization and potential future applications of the methodology are discussed for structural and functional studies on membrane proteins in a near-native environment and for characterizing protein–lipid and protein–protein interactions.

TL;DR: A detergent-free approach to isolating the tetrameric potassium channel KcsA directly from the membrane of Escherichia coli, using a styrene-maleic acid copolymer and "native nanodiscs", which enables functional characterization of the channel by electrophysiology without first depriving the protein of its native environment.

TL;DR: It was found that a collapsed conformation of the polymer is required to ensure efficient insertion into the lipid membrane and that efficient solubilization may be improved by a more homogenous distribution of the maleic acid monomer units along the polymer chain.

TL;DR: This work shows that high-resolution solid-state NMR spectra can be obtained from an integral membrane protein in native nanodiscs, as exemplified by the 2×34 kDa bacterial cation diffusion facilitator CzcD.

TL;DR: It is found that SMA displays no significant lipid preference in homogeneous binary lipid mixtures in the fluid phase, even when using lipids that by themselves show very different solubilization kinetics, and in heterogeneous phase-separated bilayers, SMA was found to have a strong preference for solubILization of lipids inThe fluid phase as compared to those in either a gel phase or a liquid-ordered phase.