The Role of Hydrophobic Interactions in the Swelling of Elastin

  • John M. Gosline
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 79)


The volume of water-swollen elastin varies dramatically with temperature, and it has been suggested that this swelling behaviour is due to changes in the strength of hydrophobic interactions between the numerous non-polar groups in the elastin protein. In this study Flory-Rehner Theory for network swelling has been used to test this hypothesis and to determine if hydrophobic interactions alone can quantitatively account for the observed volume changes. Calculated values for the solvent-polymer interaction parameter, χl derived from swelling data have been compared with independent values for the free energy of interaction between water and non-polar groups. Results indicate that the swelling changes can be attributed entirely to changes in the hydration of non-polar groups. Presumably, peptide groups and other polar regions are fully hydrated under all conditions studied.


Hydrophobic Interaction Free Energy Change Random Network Polymer Segment Elastic Mechanism 
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  1. 1.
    Gosline, J.M. (1975) Intern. Rev. Connect. Tissue Res. 7:211–249.Google Scholar
  2. 2.
    Grut, N. & McCrum, N.G. (1974) Nature, 251: 165.CrossRefGoogle Scholar
  3. 3.
    Hoeve, C.A.J. & Flory, P.J. (1974) Biopolymers, 13: 677–686.PubMedCrossRefGoogle Scholar
  4. 4.
    Tanford, C. (1973) The Hydrophobic Effect, J. Wiley & Sons, New York.Google Scholar
  5. 5.
    Nemethy, G. & Scheraga, H.A. (1962) J. Phys. Chem. 66: 1773–1789.CrossRefGoogle Scholar
  6. 6.
    Flory, P.J. & Rehner, J. Jr. (1943) J. Chem. Phys. 11: 521–526.CrossRefGoogle Scholar
  7. 7.
    Flory, P.J. (1953) Principles of Polymer Chemistry, Cornell University Press, Ithaca, New York.Google Scholar
  8. 8.
    Flory, P.J. (1950) J. Chem. Phys. 18: 108–111.CrossRefGoogle Scholar
  9. 9.
    Nemethy, G. & Scheraga, H.A. (1962) J. Chem. Phys. 36: 3382–3400.CrossRefGoogle Scholar
  10. 10.
    Nemethy, G. & Scheraga, H.A. (1962) J. Chem. Phys. 36: 3401–3417.CrossRefGoogle Scholar
  11. 11.
    Partridge, S.M. (1970) in: Chemistry and Molecular Biology of the Intracellular Matrix. E.A. Balazs (ed), Academic Press, New York, p. 593–616.Google Scholar
  12. 12.
    Gotte, L., Giro, M.G., Volpin, D. & Horne, R.M. (1974) J. Ultrastruct. Res. 46.: 23–33.PubMedCrossRefGoogle Scholar
  13. 13.
    Gotte, L., Mammi, M. & Pezzin, G. (1968) in: Symposium on Fibrous Proteins. W.G. Crewther, (ed.) Butterworths, Australia, p. 236–245.Google Scholar
  14. 14.
    Serafini-Fracassini, A., Field, J.M., Spina, M., Stephens, W.G.S. & Delf, B. (1976) J. Mol. Biol., 100: 73–84.PubMedCrossRefGoogle Scholar
  15. 15.
    Gosline, J.M. (1976) Submitted to Biopolymers.Google Scholar
  16. 16.
    Weis-Fogh, T. & Andersen, S.O. (1970) Nature 227: 718–721.PubMedCrossRefGoogle Scholar
  17. 17.
    Robert, L., Robert, B.E. & Robert A.M. (1970) Exp. Gerontol. 5: 339–356.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • John M. Gosline
    • 1
  1. 1.Department of ZoologyUniversity of British ColumbiaVancouverCanada

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