Proton‐Detected Solid‐State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs. Issue 9 (27th January 2017)

• Record Type: Journal Article
• Authors: Bersch, Beate; Dörr, Jonas M.; Hessel, Audrey; Killian, J. Antoinette; Schanda, Paul
• Is Part Of: Angewandte Chemie international edition. Volume 56:Issue 9(2017)
• Page Start: 2508
• Page End: 2512
• Publication Date: 2017-01-27
• Subjects: coplymers -- membrane proteins -- nanodiscs -- NMR spectroscopy -- solid-state NMR; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201610441
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The structure, dynamics, and function of membrane proteins are intimately linked to the properties of the membrane environment in which the proteins are embedded. For structural and biophysical characterization, membrane proteins generally need to be extracted from the membrane and reconstituted in a suitable membrane‐mimicking environment. Ensuring functional and structural integrity in these environments is often a major concern. The styrene/maleic acid co‐polymer has recently been shown to be able to extract lipid/membrane protein patches directly from native membranes to form nanosize discoidal proteolipid particles, also referred to as native nanodiscs. In this work, we show 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. Abstract : It's a kind of magic : High‐resolution magic‐angle spinning NMR spectra were obtained for the 2×34 kDa bacterial cation diffusion facilitator CzcD, following direct extraction of the membrane protein from the native membrane using a styrene/maleic acid co‐polymer to form native nanodiscs.