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Biophys J. Oct 1982; 40(1): 33–39.
PMCID: PMC1328970

Role of diffusion in ligand binding to macromolecules and cell-bound receptors.

Abstract

The association and dissociation rates of partially diffusion-controlled bimolecular reactions are considered. A simple expression for the equilibrium constant is derived using classical statistical mechanics. The relationship is established between the Collins-Kimball treatment, which is based on the "radiation" boundary condition involving an intrinsic rate constant k, and the kinetic scheme A + B in equilibrium A . . . B in equilibrium AB where A . . . B is an encounter complex. It is shown that with the appropriate choice of the interaction potential, Debye's expression for the association rate constant becomes identical to that obtained using the radiation boundary condition if k is evaluated using Kramers' theory of diffusive barrier crossing. Finally, the competitive binding of ligand to a spherical cell, whose surface is partially covered by multiple reactive sites, is studied by treating the cell as a partially reacting sphere.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Hill TL. Effect of rotation on the diffusion-controlled rate of ligand-protein association. Proc Natl Acad Sci U S A. 1975 Dec;72(12):4918–4922. [PMC free article] [PubMed]
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