State of Association of Membrane Proteins

  • Charles Tanford
Part of the Nobel Foundation Symposia book series (NOFS, volume 34)


The native environment of a membrane protein can be closely simulated by the small micelles formed by appropriate detergents. This permits solubilization of membrane proteins with retention of their native structure and biological activity. Molecular weights and polypeptide chain compositions can then be determined by well-established methods of solution physical chemistry. We have found that some membrane proteins (e.g., cytihrome b5) are monomeric, whereas others are oligomeric. The Ca++-stimulated ATPase from sarcoplasmic reticulum appears to be a trimer (possibly tetramer) of identical polypeptide chains. Each chain has two very similar halves, which suggests that the trans-membrane portion of this protein consists of six (possibly eight) symmetrically arranged elemetIT, which perhaps create an aqueous channel for the passage of Ca++ ions through the membrane.


Sodium Dodecyl Sulfate Sarcoplasmic Reticulum Polypeptide Chain Phospholipid Bilayer Phospholipid Vesicle 
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  1. Casassa, E.F. and H. Eisenberg, Advan. Protein Chem. 19, 287, (1964).CrossRefGoogle Scholar
  2. Grefrath, S.P., Ph.D. thesis, Duke University, (1974).Google Scholar
  3. Grefrath, S.P. and J.A. Reynolds, Proc. Natl. Acad. Sci. USA 71, 3913, (1974).CrossRefGoogle Scholar
  4. Hardwicke, P.M.D., and N.M. Green, Eur. J. Biochem. 42, 183, (1974). Helenius, A., and K. Simons, Biochim. Biophys. Acta 415, 29, (1975).Google Scholar
  5. Henderson, R. and P.N.T. Unwin, Nature 257, 28, (1975). Huang, C., Biochemistry 8, 344 (1969).Google Scholar
  6. Inouye, M., Proc. Natl. Acad. Sci. USA 71, 2396, (1974).CrossRefGoogle Scholar
  7. Klotz, I.M., D.W. Darnall and N.R. Langerman, The Proteins, edited by H. Neurath and R.L. Hill, vol. 1, ch. 5, Academic Press, New York (1975).Google Scholar
  8. le Maire, M., J.V. Miller and C. Tanford, Biochemistry 15, in press (1976).Google Scholar
  9. Makino, S., J.A. Reynolds and C. Tanford, J. Biol. Chem. 248, 4926, (1973).PubMedGoogle Scholar
  10. Makino, S., J.L. Woolford, C. Tanford, R.E. Webster, J. Biol. Chem. 250, 4327, (1975).PubMedGoogle Scholar
  11. Martonosí, A., J. Biol.-Chem. 243, 71, (1968).PubMedGoogle Scholar
  12. Meissner, G. and S. Fleischer, Biochem. Biophys. Res. Commun. 52, 913, (1973).CrossRefGoogle Scholar
  13. Meissner, G., G.E. Conner, and S. Fleischer, Biochim. Biophys. Acta 298, 246, (1973).CrossRefGoogle Scholar
  14. Nozaki, Y., B.K. Chamberlain, R.E. Webster and C. Tanford, Nature 259, 335, (1976).PubMedCrossRefGoogle Scholar
  15. Pinto da Silva, P. and G.L. Nicolson, Biochim. Biophys. Acta 363, 311, (1974).CrossRefGoogle Scholar
  16. Racker, E. and E. Eytan, J. Biol. Chem. 250, 7533, (1975). Rizzolo, L.J., M. le Maire, J.A. Reynolds and C. Tanford, Biochemistry 15, in press, (1976).Google Scholar
  17. Robinson, N.C. and C. Tanford, Biochemistry 14, 369, (1975). Rogers, M.J. and P. Strittmatter, J. Biol. Chem. 250, 5713, (1975).Google Scholar
  18. Shamoo, A.E., T.E. Ryan, P.S. Stewart and D.H. MacLennan, Biophys. J. 16, 109a, (1976).Google Scholar
  19. Strittmatter, P., M.J. Rogers and L. Spatz, J. Biol. Chem. 247 7188, (1972).PubMedGoogle Scholar
  20. Tanford, C., J. Phys. Chem. 78, 2469, (1974).CrossRefGoogle Scholar
  21. Tanford, C., Y. Nozaki, J.A. Reynolds and S. Makino, Biochemistry 13, 2369, (1974).PubMedCrossRefGoogle Scholar
  22. Thorley-Lawson, D.A. and N.M. Green, Eur. J. Biochem. 59, 193, (1975).PubMedCrossRefGoogle Scholar
  23. Visser, L., N.C. Robinson and C. Tanford, Biochemistry 14, 1194, (1975).PubMedCrossRefGoogle Scholar
  24. Warren, G.B., P.A. Toon, N.J.M. Birdsall, A.G. Lee, and J.C. Metcalfe, Biochemistry 13, 5501, (1974).PubMedCrossRefGoogle Scholar
  25. Warren, G.B., P.A. Toon, N.J.M. Birdsall, A.G. Lee and J.C. Metcalfe, Proc. Natl. Acad. USA 71, 622, (1974).CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Charles Tanford
    • 1
  1. 1.Department of BiochemistryDuke University Medical Ctr.DurhamUSA

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