Advertisement

On the Folding of Bacteriorhodopsin

  • D. M. Engelman

Abstract

A great deal of effort has been expended in trying to understand the folding of soluble proteins, the tertiary structures of which have been determined in many cases. The problem has turned out to be very complex, and the current lines of study have met with only limited success. Surprisingly, the possibility of structural prediction may be greater in the case of membrane proteins, where no structures of the membrane spanning regions are yet known at high resolution. This circumstance arises as a consequence of the existence of topological and energetic constraints which place important limits on the range of secondary and tertiary structures expected for globular membrane proteins. In the following discussion, I discuss the energetic arguments as I presently view them, outlining the use of an energy calculation to identify membrane spanning regions from protein sequence information, and considering the covalent, polar, and packing considerations which may be important in the final folding of globular membrane proteins in lipid bilayers.

Keywords

Lipid Bilayer Purple Membrane Membrane Span Region Nonpolar Environment Nonpolar Region 
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.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Larsen, H. (1967) Adv. Microbiol 1, 97–132CrossRefGoogle Scholar
  2. 2.
    Stoeckenius, W. and Rowan, R. (1967) J. Cell Biol. 34, 365–393CrossRefGoogle Scholar
  3. 3.
    McClare, C.W.F. (1967) Nature 216, 766–771CrossRefGoogle Scholar
  4. 4.
    Henderson, R. (1977) Ann. Rev. Biochem. Bioeng. 6, 87–109Google Scholar
  5. 5.
    Stoeckenius, W., Lozier, R., and Bogomolni, R. (1979) Biochim. Biophys. Acta 505, 215–78Google Scholar
  6. 6.
    Lanyi, J.KTT1978) Microbiol. Rev. 4, 682–706Google Scholar
  7. 7.
    Ottolenghi, M. (1980) Adv. Photochem. 12, 97–200CrossRefGoogle Scholar
  8. 8.
    Stoeckenius, W. and Bogomolni, R. (1982) Ann. Rev. Biochem. 52, 587–616Google Scholar
  9. 9.
    Blaurock, A. and Stoeckenius, W. (1973) Nature New Biol. 233, 152–155Google Scholar
  10. 10.
    Oesterheldt, D. and Stoeckenius, W. (1973) Proc. Nat. Acad. Sci. USA 70, 2853–2857Google Scholar
  11. 11.
    Garfield, E. (1980) Curr. Contents 23 (40), 5–12Google Scholar
  12. 12.
    Unwin, P.N.T. and Henderson, R. (1975) J. Mol. Biol. 94, 425–450Google Scholar
  13. 13.
    Henderson, R. and Unwin, P.N.T. (1975) Nature 257, 28–32CrossRefGoogle Scholar
  14. 14.
    Davis, S.S., Higuchi, T. and Rytting, S. (1974) Adv. Pharmaceut. Sci. 4, 73Google Scholar
  15. 15.
    Tanford, C. (1980) The Hydrophobic Effect ( New York: J. Wily Sons )Google Scholar
  16. 16.
    Singer, S.J. (1962) Adv. Prot. Chem. 17, 1Google Scholar
  17. 17.
    Singer, S.J. (1971) in: Structure and Function of Biological Membranes ( New York: Academic Press ) p. 145Google Scholar
  18. 18.
    Reynolds, J.A., Gilbert, D.B. and Tanford, C.S. (1974) Proc. Natl. Acad. Sci. USA 71, 2925Google Scholar
  19. 19.
    Richards, F. (1977) Ann. Rev. Biophys. Bioeng. 6, 151Google Scholar
  20. 20.
    Richmond, T. and Richards, F. (1978) J. Mol. Biol. 119, 537Google Scholar
  21. 21.
    Honig, B.H. and Hubbell, W. (1984) Proc. Natl. Acad. Sci. USA 81, 5412Google Scholar
  22. 22.
    Engelman, D.M., Goldman, A. and Steitz, T.A. (1982) Meth. Enzymol 88, 81CrossRefGoogle Scholar
  23. 23.
    Engelman, D.M. and Steitz, T.A. (1984) in: The Protein Folding Problem, D. Wetlaufer, Ed. AAAS SymposiaGoogle Scholar
  24. 24.
    Huang, K.S., Bayley, H., Liao, M.J., London, E. and Khorana, H.G. (1981) J. Biol. Chem. 256, 3802Google Scholar
  25. 25.
    Liao, M-J, Huang, K.S. and Khorana, H.G. (1984) J. Biol. Chem. 259, 4200Google Scholar
  26. 26.
    Wada, A. (1976) Adv. Biophys. 9, 1Google Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • D. M. Engelman
    • 1
  1. 1.Department of Biophysics and BiochemistryYale UniversityNew HavenUSA

Personalised recommendations