Allostery without conformational change. A plausible model.

  title={Allostery without conformational change. A plausible model.},
  author={Alan H Cooper and David T. F. Dryden},
  journal={European biophysics journal : EBJ},
  volume={11 2},
A general model is presented whereby ligand-induced changes in protein dynamics could produce allosteric communication between distinct binding sites, even in the absence of a macromolecular conformational change. Theoretical analysis, based on the statistical thermodynamics of ligand binding, shows that cooperative interaction free energies amounting to several kJ . mol-1 may be generated by this means. The effect arises out of the possible changes in frequencies and amplitudes of… CONTINUE READING

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