Chain Refolding and Subunit Interactions in Enzyme Molecules Covalently Bound to a Solid Matrix

  • H. Robert Horton
  • Harold E. Swaisgood
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 42)


The biological and chemical properties of functionally active proteins are dependent upon their three-dimensional molecular structures. Insight into the role of the gene-determined primary sequence of a protein molecule in providing a thermodynamically stable tertiary structure with biological activity was obtained through the classical experiments of White, Anfinsen, and their colleagues on the renaturation of reductively denatured ribonuclease A (1–3). In these and subsequent investigations, it has been demonstrated that the acquisition of functional tertiary structures in relatively simple, single-chained protein molecules can occur spontaneously as a result of the inherent thermodynamics of the system; i.e., interactions among the linear array of amino acid residues and the molecular environment.


Amino Acid Analysis Scatchard Plot Thioglycolic Acid Subunit Interaction Guanidinium Chloride 
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. 1.
    Sela, M., White, F. H., Jr., and Anfinsen, C. B. (1957) Science 125, 691.CrossRefGoogle Scholar
  2. 2.
    White, F. H., Jr. (1961) J. Biol. Chem. 236, 1353.Google Scholar
  3. 3.
    Anfinsen, C. B., and Haber, E. (1961) J. BioZ. Chem. 236, 1361.Google Scholar
  4. 4.
    Brown, J. C., and Horton, H. R. (1972) Proc. Soc. Exp. BioZ. Med. 140, 1451.Google Scholar
  5. 5.
    Epstein, C. J., and Anfinsen, C. B. (1962) J. Biol. Chem. 237, 3464.Google Scholar
  6. 6.
    Nakagawa, Y., and Perlmann, G. E. (1970) Arch. Biochem. Biophys. 140, 464.CrossRefGoogle Scholar
  7. 7.
    Fromm, H. J. (1963) J. BioZ. Chem. 238, 2938.Google Scholar
  8. 8.
    Cho, I. C., and Swaisgood, H. (1973) Biochemistry 12, 1572.CrossRefGoogle Scholar
  9. 9.
    Cho, I. C., and Swaisgood, H. E. (1972) Biochim. Biophys. Acta 258, 675.Google Scholar
  10. 10.
    Brown, J. C., Swaisgood, H. E., and Horton, H. R. (1972) Biochem. Biophys. Res. Commun. 48, 1068.CrossRefGoogle Scholar
  11. 11.
    Ellman, G. L. (1959) Arch. Biochem. Biophys. 82, 70.CrossRefGoogle Scholar
  12. 12.
    Brown, J. C., and Horton, H. R. (1973) Federation Proc. 32, 496.Google Scholar
  13. 13.
    Anfinsen, C. B. (1973) Science 181, 223.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1974

Authors and Affiliations

  • H. Robert Horton
    • 1
  • Harold E. Swaisgood
    • 1
  1. 1.Departments of Biochemistry and Food ScienceNorth Carolina State UniversityRaleighUSA

Personalised recommendations