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Helical membrane protein conformations and their environment

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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.

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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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  1. Department of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA

    Timothy A. Cross

  2. Institute of Molecular Biophysics, Florida State University, Tallahassee, FL, 32306, USA

    Timothy A. Cross & Dylan T. Murray

  3. National High Magnetic Field Laboratory, Florida State University, Tallahassee, FL, 32310, USA

    Timothy A. Cross & Dylan T. Murray

  4. Biomembrane Structure Unit, Biochemistry Department, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK

    Anthony Watts

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Cross, T.A., Murray, D.T. & Watts, A. Helical membrane protein conformations and their environment. Eur Biophys J 42, 731–755 (2013). https://doi.org/10.1007/s00249-013-0925-x

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