Advertisement

Condensed Matter Biophysics: Structure and Dynamics of Large Biomolecules

  • D. L. Stein
Conference paper
Part of the Springer Series in Biophysics book series (BIOPHYSICS, volume 1)

Abstract

A variety of experiments, probing both static and dynamic properties of compact globular proteins such as myoglobin1–3, has provided evidence that the protein undergoes something resembling a glass transition at sufficiently low temperature, typically around 200°K. More precisely, myoglobin and several other proteins (hemoglobin, calmodulin) behave as if they possess a large number of conformational substates (CS) about a more or less fixed tertiary structure. These substates are separated by barriers whose energy scale is typically of order 200°K, the freezing temperature. Two questions which immediately come to mind are:
  1. 1.

    To what extent is the transition driven by the solvent, and to what extent is it a consequence of the internal structure of the protein itself?

     
  2. 2.

    How relevant are the low temperature (i.e., glassy) properties of the protein at higher, physiological temperatures?

     

Keywords

Glass Transition Spin Glass Physiological Temperature Spin Glass Phase Freezing Transition 
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.
    E.H. Austin, K.W. Beesem, L. Eisenstein, H. Frauenfelder, and I.C. Gunsalus, Biochemistry 14, 5355 (1975).PubMedCrossRefGoogle Scholar
  2. 2.
    H. Frauenfelder, G.A. Petsko, and D. Tsernoglou, Nature (London) 280, 558 (1979).CrossRefGoogle Scholar
  3. 3.
    F. Parak, E.N. Frolov, E.L. Mössbauer, and V.I. Goldanskii, J. Mol. Biol. 145, 824 (1981).CrossRefGoogle Scholar
  4. 4.
    J.F. Edwards and P.W. Anderson, J. Phys. F5, 965 (1975).CrossRefGoogle Scholar
  5. 5.
    D. Sherrington and S. Kirkpatrick, Phys. Eev. Lett. 35, 1792 (1975).CrossRefGoogle Scholar
  6. 6.
    E.G. Palmer, Adv. Phys. 31, 669 (1982).CrossRefGoogle Scholar
  7. 7.
    P.W. Anderson, B.I. Halperin, and C. Varma, Phil Mag. 25, 1 (1972).CrossRefGoogle Scholar
  8. 8.
    W.A. Phillips, J. Low. Temp. Phys. 7, 351 (1972).CrossRefGoogle Scholar
  9. 9.
    D.L. Stein, Proc. Nat’l Acad. Sci. USA 82, 3670 (1985).CrossRefGoogle Scholar
  10. 10.
    D.L. Stein, Proceedings of the Conference on Protein Structure: Molecular and Electronic Reactivity, Philadelphia, 1985, in press.Google Scholar
  11. 11.
    D.L. Stein, Comments on Molecular and Cellular Biophysics, in press.Google Scholar
  12. 12.
    W. Döster, E. Dunau, and E. Luscher, preprint.Google Scholar
  13. 13.
    M. Karplus, unpublished.Google Scholar
  14. 14.
    E. Shyamsunder, Ph.D. Thesis, University of Illinois, 1985 (unpublished).Google Scholar
  15. 15.
    E.H. Austin, D.L. Stein, and J. Wang, preprint.Google Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1987

Authors and Affiliations

  • D. L. Stein
    • 1
  1. 1.Dept. of PhysicsPrinceton UniversityPrincetonUSA

Personalised recommendations