ArticleBioengineering (Basel, Switzerland)2026
Toward Nanodisc Tailoring for SANS Study of Membrane Proteins.
Article in Bioengineering (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Although membrane proteins are of major importance in both physiology and disease, they remain less studied than soluble proteins due to the complex amphiphilic environments required to preserve their structure and function. As a consequence, membrane proteins are under-represented in structural databases. In this work, we present a robust structural characterization of lipid nanodiscs designed to facilitate membrane protein studies by small-angle neutron scattering. By combining small-angle X-ray and neutron scattering, we investigate nanodiscs of three different sizes and three lipid compositions to accommodate a broad range of systems. Specifically, nanodiscs with diameters of approximately 9 nm, 12 nm, and 15 nm were examined. Beyond the commonly used di-myristoyl-phosphatidylcholine lipid, we produced and characterized polar lipid extracts from a Gram-negative bacterium (
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