Structure determination of membrane proteins by nuclear magnetic resonance spectroscopy

Annu Rev Anal Chem (Palo Alto Calif). 2013;6:305-28. doi: 10.1146/annurev-anchem-062012-092631. Epub 2013 Apr 1.

Abstract

Many biological membranes consist of 50% or more (by weight) membrane proteins, which constitute approximately one-third of all proteins expressed in biological organisms. Helical membrane proteins function as receptors, enzymes, and transporters, among other unique cellular roles. Additionally, most drugs have membrane proteins as their receptors, notably the superfamily of G protein-coupled receptors with seven transmembrane helices. Determining the structures of membrane proteins is a daunting task because of the effects of the membrane environment; specifically, it has been difficult to combine biologically compatible environments with the requirements for the established methods of structure determination. There is strong motivation to determine the structures in their native phospholipid bilayer environment so that perturbations from nonnatural lipids and phases do not have to be taken into account. At present, the only method that can work with proteins in liquid crystalline phospholipid bilayers is solid-state NMR spectroscopy.

Publication types

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

MeSH terms

  • Lipid Bilayers / chemistry
  • Membrane Proteins / chemistry*
  • Micelles
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Phospholipids / chemistry
  • Protein Structure, Secondary
  • Receptors, G-Protein-Coupled / chemistry*
  • Receptors, Interleukin-8A / chemistry

Substances

  • Lipid Bilayers
  • Membrane Proteins
  • Micelles
  • Phospholipids
  • Receptors, G-Protein-Coupled
  • Receptors, Interleukin-8A