Membrane proteins in their native habitat as seen by solid-state NMR spectroscopy

Protein Sci. 2015 Sep;24(9):1333-46. doi: 10.1002/pro.2700. Epub 2015 May 27.


Membrane proteins play many critical roles in cells, mediating flow of material and information across cell membranes. They have evolved to perform these functions in the environment of a cell membrane, whose physicochemical properties are often different from those of common cell membrane mimetics used for structure determination. As a result, membrane proteins are difficult to study by traditional methods of structural biology, and they are significantly underrepresented in the protein structure databank. Solid-state Nuclear Magnetic Resonance (SSNMR) has long been considered as an attractive alternative because it allows for studies of membrane proteins in both native-like membranes composed of synthetic lipids and in cell membranes. Over the past decade, SSNMR has been rapidly developing into a major structural method, and a growing number of membrane protein structures obtained by this technique highlights its potential. Here we discuss membrane protein sample requirements, review recent progress in SSNMR methodologies, and describe recent advances in characterizing membrane proteins in the environment of a cellular membrane.

Keywords: cell membrane; lipid bilayer; membrane protein; protein structure; solid-state NMR.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Humans
  • Lipid Bilayers / chemistry
  • Lipid Bilayers / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / physiology*
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Protein Structure, Secondary


  • Lipid Bilayers
  • Membrane Proteins