Structure of voltage-dependent anion channel-tethered bilayer lipid membranes determined using neutron reflectivity.

ABSTRACT: Neutron reflectivity (NR) has emerged as a powerful technique to study the structure and behavior of membrane proteins at planar lipid interfaces. Integral membrane proteins (IMPs) remain a significant challenge for NR owing to the difficulty of forming complete bilayers with sufficient protein density for scattering techniques. One strategy to achieve high protein density on a solid substrate is the capture of detergent-stabilized, affinity-tagged IMPs on a nitrilotriacetic acid (NTA)-functionalized self-assembled monolayer (SAM), followed by reconstitution into the lipids of interest. Such protein-tethered bilayer lipid membranes (ptBLMs) have the notable advantage of a uniform IMP orientation on the substrate. Here, NR is used to provide a structural characterization of the ptBLM proces

SUBMITTER: Hoogerheide DP 

PROVIDER: S-EPMC6317592 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature