Enhancement of Association Rates by Nonspecific Binding to DNA and Cell Membranes
- 18 October 2004
- journal article
- research article
- Published by American Physical Society (APS) in Physical Review Letters
- Vol. 93 (17), 178101
- https://doi.org/10.1103/physrevlett.93.178101
Abstract
A comprehensive analytic theory is developed for the kinetics of reversible association with specific sites on DNA and receptors on cell membranes in the presence of nonspecific binding to the target surfaces. Nonspecific binding is treated as a short-range attractive potential, which is more fundamental and realistic than the surface sliding model. The presence of a surface potential around the target enhances the rate of specific association and for reversible reactions leads to deviations from single exponential relaxation.Keywords
This publication has 12 references indexed in Scilit:
- Kinetics of reversible diffusion influenced reactions: The self-consistent relaxation time approximationThe Journal of Chemical Physics, 2002
- Electrostatic Control of the Membrane Targeting of C2 DomainsMolecular Cell, 2002
- Long-Time Tails in the Kinetics of Reversible Bimolecular ReactionsPhysical Review Letters, 2001
- Enhancement of protein-protein association rate by interaction potential: accuracy of prediction based on local Boltzmann factorBiophysical Journal, 1997
- Brownian dynamics study of the influences of electrostatic interaction and diffusion on protein-protein association kineticsBiophysical Journal, 1993
- Orientation constraints in diffusion-limited macromolecular association. The role of surface diffusion as a rate-enhancing mechanismBiophysical Journal, 1985
- Stochastically gated diffusion-influenced reactionsThe Journal of Chemical Physics, 1982
- Association kinetics with coupled three- and one-dimensional diffusionBiophysical Chemistry, 1982
- Diffusion-controlled bimolecular reaction rates. The effect of rotational diffusion and orientation constraintsBiophysical Journal, 1981
- Effect of rotation on the diffusion-controlled rate of ligand-protein association.Proceedings of the National Academy of Sciences, 1975