Membrane Protein Structure Determination by Deuterium-NMR Case Study: Retinal in Bacteriorhodopsin

  • Anne S. Ulrich
  • Anthony Watts
Conference paper
Part of the NATO ASI Series book series (volume 63)


To understand the function of a protein, one needs to establish the relationship between its three-dimensional structure, its dynamics and its environment. For many soluble proteins the primary, secondary and tertiary structures have been described in considerable detail, but a crucial gap in our knowledge is still the molecular structure of membrane proteins. These cannot usually be investigated by diffraction methods, because their amphipathic nature makes crystallization inherently difficult.


Nuclear Magnetic Resonance Quadrupole Splitting Purple Membrane Extracellular Side Thermal Isomerization 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Ceska T.A. & Henderson R. (1990) J. Mol. Biol. 213, 539–560PubMedCrossRefGoogle Scholar
  2. Clark N. A., Rothschild K. J., Luippold D. A. & Simon B. A. (1980) Biophys. J. 31, 65–96PubMedCrossRefGoogle Scholar
  3. Creuzet, F., McDermott, A., Gebhard, R., van der Hoef, K., Spijker-Assink, M. B., Herzfeld, J., Lugtenburg, J., Levitt, M. H. & Griffin, R. G. (1991) Science 251, 783–786PubMedCrossRefGoogle Scholar
  4. Earnest, T. N., Roepe, P., Braiman, M. S., Gillespie, J. & Rothschild, K. J. (1986) Biochem. 25, 7793–7798CrossRefGoogle Scholar
  5. Harbison, G. S., Smith, S. O., Pardoen, J. A., Winkel, C., Lugtenburg, J., Herzfeld, J., Mathies, R. & Griffin, R. G. (1984) Proc. Natl Acad. Sci. USA 81, 1706–1709PubMedCrossRefGoogle Scholar
  6. Hauß, T., Grzesiek, S., Otto, H., Westerhausen, J. & Heyn, M. P. (1990) Biochem. 29, 4904–4913CrossRefGoogle Scholar
  7. Henderson, R., Baldwin, J. M., Ceska, T. A., Zemlin, F., Beckmann E. & Downing, K.H. J. (1990) Mol. Biol 213, 899–929CrossRefGoogle Scholar
  8. Heyn, M. P., Cherry, R. J. & Müller (1977) J. Mol Biol 117, 607–620PubMedCrossRefGoogle Scholar
  9. Heyn, M. P., Westerhausen, J., Wallat, I. & Seiff, F. (1988) Proc. Natl. Sci. USA 85, 2146–2150CrossRefGoogle Scholar
  10. Huang, J. Y. & Lewis, A. (1989) Biophys. J. 55, 835–842PubMedCrossRefGoogle Scholar
  11. Lin, S. W. & Mathies, R. A. (1989) Biophys. J. 56, 653–660PubMedCrossRefGoogle Scholar
  12. Seelig, J. (1977) Q. Rev. Biophys 10, 353–418PubMedCrossRefGoogle Scholar
  13. Seiff, F., Westerhausen, J., Wallat, I. & Heyn, M. P. (1986) Proc. Natl Sci. USA 83, 7746–7750CrossRefGoogle Scholar
  14. Stam, C. H. (1972) Acta Cryst. B28, 2936–2945Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1992

Authors and Affiliations

  • Anne S. Ulrich
    • 1
  • Anthony Watts
    • 1
  1. 1.Department of BiochemistryUniversity of OxfordOxfordEngland

Personalised recommendations