Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs

Angew Chem Int Ed Engl. 2017 Feb 20;56(9):2508-2512. doi: 10.1002/anie.201610441. Epub 2017 Jan 27.


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.

Keywords: NMR spectroscopy; coplymers; membrane proteins; nanodiscs; solid-state NMR.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Cupriavidus / chemistry*
  • Diffusion
  • Maleates / chemistry*
  • Membrane Transport Proteins / chemistry*
  • Nanostructures / chemistry
  • Polystyrenes / chemistry*
  • Proteolipids / chemistry
  • Proton Magnetic Resonance Spectroscopy / methods*
  • Protons
  • Zinc / chemistry


  • Bacterial Proteins
  • Maleates
  • Membrane Transport Proteins
  • Polystyrenes
  • Proteolipids
  • Protons
  • styrene-maleic acid polymer
  • Zinc