On the Role of the Conformation Changes at the Active Site for Allosteric Interactions

  • V. Kavardjikov
  • I. Zlatanov


In the existing theoretical works on the allosteric interactions in proteins only the subunit interactions are considered without taking into account the conformation changes in the active sites themselves. The present paper is an effort to take into consideration the role of the fine conformation changes in the allosteric interactions at the active sites. The respective correction factors to the rate constants of ligand binding in the equation of saturation (Eq. of Adair) have been found. The mathematical formalism for the fluctuation equilibrium between, a number of conformation states of the active site with different ligand affinities has been obtained.


Free Energy Conformation Change Activation Free Energy Subunit Interaction Conformation State 
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.
    Monod J., Wyman J., Changeux J. P. J. Mol. Biol. 12, (1965) 88PubMedCrossRefGoogle Scholar
  2. 2.
    Koshland D.E., Nematy G., Filmer D., Biochemistry 5, (1966) 365PubMedCrossRefGoogle Scholar
  3. 3.
    Adair G.S., J. Biol. Chem. 6 3, (1925) 529Google Scholar
  4. 4.
    Pauling D., Proc. Nat. Acad.Sci. USA 21, (1935) 186PubMedCrossRefGoogle Scholar
  5. 5.
    Frieden C., J. Biol. Chem. 242, (1967) 4045.PubMedGoogle Scholar
  6. 6.
    Ricard J., Mouttet C., Nari J., Europ. J. Biochem. 41, (1974) 479–497.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1975

Authors and Affiliations

  • V. Kavardjikov
    • 1
  • I. Zlatanov
    • 1
  1. 1.Central Laboratory of BiophysicsBulgarian Academy of SciencesSofiaBulgaria

Personalised recommendations