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Noncooperative thermodynamics and kinetic models of ligand binding to polymers: Connecting McGhee–von Hippel model with the Tonks gas model
Author(s) -
J.P.G. Villaluenga,
Jules Vidal,
Francisco J. Cao
Publication year - 2020
Publication title -
physical review. e
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.896
H-Index - 304
eISSN - 2470-0053
pISSN - 2470-0045
DOI - 10.1103/physreve.102.012407
Subject(s) - kinetic energy , ligand (biochemistry) , thermodynamics , chemical reaction , ideal gas , chemical equilibrium , polymer , chemistry , computational chemistry , chemical physics , physics , classical mechanics , organic chemistry , biochemistry , receptor
Ligand binding to polymers modifies the physical and chemical properties of the polymers, leading to physical, chemical, and biological implications. McGhee and von Hippel obtained the equilibrium coverage as a function of the ligand affinity, through the computation of the possible binding sites for the ligand. Here, we complete this theory deriving the kinetic model for the ligand-binding dynamics and the associated equilibrium chemical potential, which turns out to be of the Tonks gas model type. At low coverage, the Tonks chemical potential becomes the Fermi chemical potential and even the ideal gas chemical potential. We also discuss kinetic models associated with these chemical potentials. These results clarify the kinetic models of ligand binding, their relations with the chemical potentials, and their range of validity. Our results highlight the inaccuracy of ideal and simplified kinetic approaches for medium and high coverages.

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