AI Article Synopsis
- A two-dimensional NMR spectrum of an integral membrane protein (IMP) was obtained using nanodiscs, which create a more native-like environment compared to previous methods that used detergents or organic solvents.
- Nanodiscs, smaller 150 kDa membrane models, effectively solubilize IMPs, allowing them to tumble isotropically, a requirement for effective NMR analysis.
- The study successfully incorporated the 70 residue polypeptide CD4mut into the nanodiscs, demonstrating good signal quality in NMR, thus confirming the suitability of this method for studying IMPs.
Article Abstract
We present a two-dimensional solution NMR spectrum of an integral membrane protein (IMP) in a nanodisc. Solution NMR relies on rapid isotropic tumbling of the analyte with correlation times in the nanosecond range. IMPs in a cellular membrane do not satisfy this condition. Previous liquid-state NMR studies on IMPs were conducted in organic solvent or artificial membrane mimicking particles like detergent micelles. Nanodiscs are relatively small (150 kDa), detergent-free model membranes that are suitable for functional reconstitution of IMPs. Nanodiscs allow solubilization of integral membrane proteins in a nearly native lipid bilayer environment. The 70 residue polypeptide CD4mut was incorporated into nanodiscs. CD4mut features one transmembrane helix. The aliphatic (1)H-(13)C HSQC spectrum of nanodiscs with inserted, ((13)C, (15)N)-labeled CD4mut exhibits reasonably dispersed protein and lipid NMR signals. Our results demonstrate that IMPs in nanodiscs are amenable to liquid-state NMR methodology.
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