The Interaction of Intrinsic Proteins and Lipids in Biomembranes

  • D. Chapman
  • J. C. Gomez-Fernandez
  • F. M. Goni
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 71)


The concept that biomembranes are built on a lipid bilayer matrix is now commonly accepted. Suggestions have been made that non-lamellar regions may also occur within the structure of natural biomembranesl, although this view is presently somewhat controversial2,3. The proteins associated with biomembranes are located either within the lipid matrix (intrinsic proteins) or attached to the hydrophilic faces of the bilayer (extrinsic proteins). In some instances, intrinsic proteins may be held in position by a cytoskeleton.


Quadrupole Splitting Spin Label Intrinsic Protein Lipid Matrix High Protein Concentration 
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  1. 1.
    B. de Kruijff, P.R. Cullis and A.J. Verkeij, Trends in Biochem. Sci. 5, 79–81 (1980).CrossRefGoogle Scholar
  2. 2.
    A.J. Deese, E.A. Dratz and M.F. Brown, FEBS Lett. 124, 92–99 (1981).CrossRefGoogle Scholar
  3. 3.
    S.W. Hui, and T.P. Stewart, Nature (London) 290, 427 (1981).CrossRefGoogle Scholar
  4. 4.
    D. Chapman, J.C. Gomez-Fernandez and F.M. Goni, FEBS Lett. 98, 211–223 (1979).PubMedCrossRefGoogle Scholar
  5. 5.
    P.C. Jost, O.H. Griffith, R.A. Capaldi and G. Vanderkooi, Proc. Nat. Acad. Sci. U.S.A. 70, 480–484 (1973).CrossRefGoogle Scholar
  6. 6.
    T.R. Hesketh, G.A. Smith, M.D. Houslay, K.A. McGill, N.J.M. Birdsall, J.C. Metcalfe and G.B. Warren, Biochemistry 15, 4145–4151 (1976).PubMedCrossRefGoogle Scholar
  7. 7.
    M.F. Brown, G.P. Miljanich and E.A. Dratz, Biochemistry 16, 2640–2648 (1977).PubMedCrossRefGoogle Scholar
  8. 8.
    E. Oldfield, R. Gilmore, M. Glaser, H.S. Gutowski, J.C. Hschung, S. Kang, M. Meadows and D. Rice, Proc. Nat. Acad. Sci. U.S.A. 75, 4657–4660 (1978).CrossRefGoogle Scholar
  9. 9.
    A. Seelig and J. Seelig, Hoppe Seyler’s Z. Physiol. Chem. 359, 1747–1756 (1978).PubMedCrossRefGoogle Scholar
  10. 10.
    D. Rice, M.D. Meadows, A.O. Scheinman, F.M. Goni, J.C. Gomez-Fernandez, M.A. Moscarello, D. Chapman and E. Oldfield, Biochemistry, 18, 5893–5903 (1979).PubMedGoogle Scholar
  11. 11.
    D. Rice and E. Oldfield, Biochemistry 18, 3272–3279 (1979).PubMedCrossRefGoogle Scholar
  12. 12.
    H. Traube and E. Sackmann, J. Am. Chem. Soc. 94, 4499–4510 (1972).CrossRefGoogle Scholar
  13. 13.
    D.A. Pink, A. Georgallas and D. Chapman, Biochemistry 20, 7152–7157 (1981).PubMedCrossRefGoogle Scholar
  14. 14.
    W. Hoffmann, D.A. Pink, C.J. Restall and D. Chapman, Eur. J. Biochem. 114, 585–589 (1981).PubMedCrossRefGoogle Scholar
  15. 15.
    J.C. Gomez-Fernandez, F.M. Goni, D. Bach, C.J. Restall and D. Chapman, Biochim. Biophys Acta 598, 502–516 (1980).PubMedCrossRefGoogle Scholar
  16. 16.
    A. Alonso, C.J. Restall, M. Turner, J.C. Gomez-Fernandez, F.M. Goni and D. Chapman, Biochim. Biophys. Acta 689, 283–289 (1982).CrossRefGoogle Scholar
  17. 17.
    W. Hoffmann, M.G. Sarzala, J.C. Gomez-Fernandez, F.M. Goni, C.J. Restall, D. Chapman, G. Heppeler and W. Kreutz, J. Mol. Biol. 141, 119–132 (1980).PubMedCrossRefGoogle Scholar
  18. 18.
    H. Sandermann Jr, Biochim. Biophys. Acta 515, 209–237 (1978).PubMedGoogle Scholar
  19. 19.
    W.L. Dean and C. Tanford, J. Biol. Chem. 252, 3351–3353 (1977).Google Scholar

Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • D. Chapman
    • 1
  • J. C. Gomez-Fernandez
    • 1
  • F. M. Goni
    • 1
  1. 1.Royal Free Hospital School of MedicineLondonUK

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