The use of amphipols for solution NMR studies of membrane proteins: advantages and constraints as compared to other solubilizing media

J Membr Biol. 2014 Oct;247(9-10):827-42. doi: 10.1007/s00232-014-9654-z. Epub 2014 Mar 28.


Solution-state nuclear magnetic resonance studies of membrane proteins are facilitated by the increased stability that trapping with amphipols confers to most of them as compared to detergent solutions. They have yielded information on the state of folding of the proteins, their areas of contact with the polymer, their dynamics, water accessibility, and the structure of protein-bound ligands. They benefit from the diversification of amphipol chemical structures and the availability of deuterated amphipols. The advantages and constraints of working with amphipols are discussed and compared to those associated with other non-conventional environments, such as bicelles and nanodiscs.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Artifacts
  • Cell Membrane / chemistry*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Lipid Bilayers / chemistry*
  • Magnetic Resonance Spectroscopy / methods*
  • Membrane Proteins / chemistry*
  • Polymers / chemistry*
  • Solubility
  • Solutions
  • Surface-Active Agents / chemistry*
  • Technology Assessment, Biomedical
  • Water / chemistry


  • Lipid Bilayers
  • Membrane Proteins
  • Polymers
  • Solutions
  • Surface-Active Agents
  • Water