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European Biophysics Journal

, Volume 42, Issue 10, pp 731–755 | Cite as

Helical membrane protein conformations and their environment

  • Timothy A. CrossEmail author
  • Dylan T. Murray
  • Anthony Watts
Review

Abstract

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.

Keywords

Membrane proteins Solid-state NMR Lipids Membrane protein crystallography 

Notes

Acknowledgments

This review was in part supported by Florida State University in a sabbatical for T.A.C. In addition, partial support was provided by NIH grants AI 074805, AI 073891, and AI 023007 and the National Science Foundation through Cooperative Agreement 0654118 between the Division of Materials Research and the State of Florida. A.W. was supported by the Medical Research Council (MRC) and the Engineering and Physical Sciences Research Council (EPSRC), UK.

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Copyright information

© European Biophysical Societies' Association 2013

Authors and Affiliations

  • Timothy A. Cross
    • 1
    • 2
    • 3
    Email author
  • Dylan T. Murray
    • 2
    • 3
  • Anthony Watts
    • 4
  1. 1.Department of Chemistry and BiochemistryFlorida State UniversityTallahasseeUSA
  2. 2.Institute of Molecular BiophysicsFlorida State UniversityTallahasseeUSA
  3. 3.National High Magnetic Field LaboratoryFlorida State UniversityTallahasseeUSA
  4. 4.Biomembrane Structure Unit, Biochemistry DepartmentUniversity of OxfordOxfordUK

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