Helical membrane protein conformations and their environment

Eur Biophys J. 2013 Oct;42(10):731-55. doi: 10.1007/s00249-013-0925-x. Epub 2013 Sep 1.


Evidence that membrane proteins respond conformationally and functionally to their environment is growing. Structural models, by necessity, have been characterized in preparations where the protein has been removed from its native environment. Different structural methods have used various membrane mimetics that have recently included lipid bilayers as a more native-like environment. Structural tools applied to lipid bilayer-embedded integral proteins are informing us about important generic characteristics of how membrane proteins respond to the lipid environment as compared with their response to other nonlipid environments. Here, we review the current status of the field, with specific reference to observations of some well-studied α-helical membrane proteins, as a starting point to aid the development of possible generic principles for model refinement.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Review

MeSH terms

  • Cell Membrane / metabolism
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Membranes, Artificial
  • Protein Structure, Secondary
  • Protein Structure, Tertiary


  • Membrane Proteins
  • Membranes, Artificial