Correlation between Structural Conformations at Different Levels in Hemoglobin Determined by XANES

  • A. Bianconi
  • A. Congiu Castellano
  • S. Della Longa
Part of the NATO ASI Series book series (NSSB, volume 263)


The interaction between the structural conformations occurring at different levels of the protein organization is of key importance in understanding the dynamics of the biological molecules. Hemoglobin is studied here because it provides a good system to investigate fundamental aspects of biomolecules. In hemoglobin we can distinguish three levels of the protein organization 1) the quaternary structure of the tetramer, 2) the tertiary structure of the subunits, 3) the local structure of the Fe site in the heme.


Oxygen Affinity Clofibric Acid Structural Conformation Allosteric Effector Electron Storage Ring 
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.
    M. F. Perutz, Quat. Rev. Biophysics 22, 139 (1989)CrossRefGoogle Scholar
  2. 2.
    K. Imai, Allosteric Effects in Haemoglobin, Cambridge Univesrsity Press, (1982)Google Scholar
  3. 3.
    J. M. Baldwin and C. Chothia, J. Mol. Biol. 129, 183 (1979)CrossRefGoogle Scholar
  4. 4.
    B. R. Gelin, A. W. Lee, and M. Karplus. J. Mol Biol. 171, 489 (1983)CrossRefGoogle Scholar
  5. 5.
  6. 6.
  7. 7.
    A. Bianconi, A. Congiu Castellano, P. J. Durham, S. S. Hasnain and S. Phillips, Nature 318, 685 (1985)ADSCrossRefGoogle Scholar
  8. 8.
    A. Bianconi in “X-ray absorption: principle, applications, techniques of EXAFS, SEXAFS, XANES” ed. R. Prinz and D. Koningsberger, (J. Wiley and sons, New York, 1988)Google Scholar
  9. 9.
    A. Bianconi, A. Congiu-Castellano, eds, “Biophysics and synchrotron radiation” (Springer Verlag, Berlin, 1987)Google Scholar
  10. 10.
    A. Arnone and M. F. Perutz, Nature 249, 34 (1974)ADSCrossRefGoogle Scholar
  11. 11.
    M. F. Perutz, G. Fermi, D. J. Abraham, C. Poyrat, and E. Bursaux, J. Am. Chem. Soc. 108, 1064 (1986)CrossRefGoogle Scholar
  12. 12.
    G. Amiconi, R. Santucci, M. Coletta, A. Congiu Castellano, A. Giovannelli, M. Dell’Ariccia, S. Delia Longa, M. Barteri, E. Burattini and A. Bianconi, Biochemistry 28, 8547 (1989)CrossRefGoogle Scholar
  13. 13.
    S. Delia Longa, A. Bianconi, A. Congiu Castellano, to be published.Google Scholar

Copyright information

© Springer Science+Business Media New York 1991

Authors and Affiliations

  • A. Bianconi
    • 1
    • 2
  • A. Congiu Castellano
    • 2
  • S. Della Longa
    • 1
    • 2
  1. 1.Dipartimento di Medicina SperimentaleUniversità dell’AquilaL’AquilaItaly
  2. 2.Biostructure Research unit of GNCB, CNR, Dipartimento di FisicaUniversità di Roma “La Sapienza”RomaItaly

Personalised recommendations