Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding

@article{Galletto2005KineticsOA,
  title={Kinetics of allosteric conformational transition of a macromolecule prior to ligand binding},
  author={Roberto Galletto and Maria J. Jezewska and Wlodzimierz Bujalowski},
  journal={Cell Biochemistry and Biophysics},
  year={2005},
  volume={42},
  pages={121-144}
}
Two fundamentally different mechanisms of ligand binding are commonly encountered in biological kinetics. One mechanism is a sequential multistep reaction in which the bimolecular binding step is followed by first-order steps. The other mechanism includes the conformational transition of the macromolecule, before the ligand binding, followed, by the ligand binding process to one of the conformational states. In stopped-flow kinetic studies, the reaction mechanism is established by examining the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-9 of 9 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 32 references

Relaxation Kinetics

  • C. J. Bernasconi
  • 1976
Highly Influential
10 Excerpts

Kinetics and mechanism for the conformational transition in pguanidinobenzoate bovine trypsinogen induced by the isoleucine-valine dipeptide

  • H. J. Nolte, E. Neuman
  • Biophys. Chem
  • 1979
Highly Influential
5 Excerpts

Similar Papers

Loading similar papers…