Conformational dynamics of proteins: beyond the nanosecond time scale

  • H. Grubmüller
  • N. Ehrenhofer
  • P. Tavan
Part of the Centre de Physique des Houches book series (LHWINTER, volume 2)

Abstract

Protein motions and functional processes in proteins occur on a wide range of time scales. The fastest atomic motions take place on a femtosecond time scale. Fast biochemical reactions like the primary steps in photosynthesis last few picoseconds. Most biochemical reactions like enzymatic processes take much longer — microseconds or even few milliseconds. They are often accompanied by larger structural rearrangements in the protein, called conformational transitions[l], which are characterized by transition times of nanoseconds or much longer. A prominent example for an extremely slow conformational transition, with a transition time of many years, is the one which is believed to be responsible for the pathogenic effect of prions[2]. Often, conformational transitions constitute functional important motions, as for the gating of channel proteins or in protein folding.

Keywords

Assure Photosynthesis Macromolecule Braunstein Rase 

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References

  1. [1]
    A. Ansari, J. Berendzen, D. Braunstein, B. R. Cowen, H. Frauenfelder, M. K. Hong, I. E. T. Iben, J. B. Johnson, P. Ormos, T. B. Sauke, R. Scholl, A. Schulte, P. J. Steinbach, J. Vittitow, R. D. Young, Biophys. Chem. 26 (1987) 337.CrossRefGoogle Scholar
  2. [2]
    D. A. Kocisko, et al., Nature 370 (11 Aug 1994) 471.CrossRefADSGoogle Scholar
  3. [3]
    J. A. McCammon, B. R. Celin, M. Karplus, Nature 267 (1977) 585.CrossRefADSGoogle Scholar
  4. [4]
    B. R. Brooks, R. E. Bruccoleri, B. D. Olafson, D. J. States, S. Swaminathan, M. Karplus, J. Comp. Chem. 4 (1983) 187.CrossRefGoogle Scholar
  5. [5]
    W. F. van Gunsteren, H. J. C. Berendsen, Angew. Chem. Int. Ed. Engl. 29 (1990) 992.CrossRefGoogle Scholar
  6. [6]
    M. Levitt, S. Lifson, J. Molec. Biol. 46 (1969) 269.CrossRefGoogle Scholar
  7. [7]
    H. Frauenfelder, S. G. Sligar, P. G. Wolynes, Science 254 (1991) 1598.CrossRefADSGoogle Scholar
  8. [8]
    H. Grubmüller, P. Tavan, J. Chem. Phys. (Sept. 1994). In press.Google Scholar
  9. [9]
    H. Grubmüller, thesis, Technische Universität München (Jan. 1994).Google Scholar
  10. [10]
    H. Frauenfelder, Biophys. J. 47 (1985) 35.Google Scholar
  11. [11]
    R. Elber, M. Karplus, Science 235 (1987) 318.CrossRefADSGoogle Scholar
  12. [12]
    N. Go, T. Noguti, Chem. Scr. 29A (1989) 151.Google Scholar
  13. [13]
    N. Ehrenhofer, thesis, Ludwig-Maximilians-Universität München (1994).Google Scholar
  14. [14]
    A. Ansari, J. Berendzen, S. F. Browne, H. Frauenfelder, I. E. T. Iben, T. B. Sauke, E. Shyamsunder, R. D. Young, Proc. Natl. Acad. Sci. USA 82 (1985) 5000.CrossRefADSGoogle Scholar
  15. [15]
    D. R. Dersch, P. Tavan, “Control of annealing in minimal free energy vector quantization”, Proceedings of the IEEE International Conference on Neural Networks ICNN’94, S. K. Orlando, Florida, June 28-July 2, 1994, Rogers and D. W. Ruck, Eds. (IEEE, Piscataway, U.S.A, 1994) pp. 698–703.Google Scholar
  16. [16]
    K. V. Mardia, J. T. Kent, J. M. Bibby, “Multivariate Analysis” (Academic Press, London, 1979).MATHGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 1995

Authors and Affiliations

  • H. Grubmüller
    • 1
  • N. Ehrenhofer
    • 1
  • P. Tavan
    • 1
  1. 1.Institut für Medizinische OptikUniversität MünchenMünchenGermany

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