Nanodiscs versus macrodiscs for NMR of membrane proteins

Biochemistry. 2011 Oct 25;50(42):8983-5. doi: 10.1021/bi201289c. Epub 2011 Sep 30.


It is challenging to find membrane mimics that stabilize the native structures, dynamics, and functions of membrane proteins. In a recent advance, nanodiscs have been shown to provide a bilayer environment compatible with solution NMR. We show that increasing the lipid to "belt" peptide ratio expands their diameter, slows their reorientation rate, and allows the protein-containing discs to be aligned in a magnetic field for oriented sample solid-state NMR. The spectroscopic properties of membrane proteins with one to seven transmembrane helices in q = 0.1 isotropic bicelles, ~10 nm diameter isotropic nanodiscs, ~30 nm diameter magnetically aligned macrodiscs, and q = 5 magnetically aligned bicelles are compared.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacteriorhodopsins / chemistry
  • Crystallography, X-Ray / methods
  • Lipid Bilayers / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Membrane Proteins / chemistry*
  • Membranes, Artificial*
  • Molecular Mimicry


  • Bacterial Proteins
  • Lipid Bilayers
  • Membrane Proteins
  • Membranes, Artificial
  • Bacteriorhodopsins