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Exact analysis of ligand-induced dimerization of monomeric receptors.

ABSTRACT: This paper analyzes the equilibria involved in the dimerization of monomeric receptors with homo-bifunctional ligands. We provide analytical expressions that can be used to estimate the concentration of each species present in a mixture of homo-bifunctional ligand and monomeric proteins, given initial conditions defining the total concentration of bivalent ligand [L2]0, the total concentration of protein [P]0, one dissociation constant Kd, and a parameter to account for cooperativity alpha. We demonstrate that the fraction of protein present in a complex of two proteins and one bivalent ligand (P x L2 x P) is maximized at [L2]0 = Kd/2 + [P]0/2.

SUBMITTER: Mack ET

PROVIDER: S-EPMC2754295 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature

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Exact analysis of ligand-induced dimerization of monomeric receptors.

Mack Eric T ET Perez-Castillejos Raquel R Suo Zhigang Z Whitesides George M GM

Analytical chemistry 20080611 14

This paper analyzes the equilibria involved in the dimerization of monomeric receptors with homo-bifunctional ligands. We provide analytical expressions that can be used to estimate the concentration of each species present in a mixture of homo-bifunctional ligand and monomeric proteins, given initial conditions defining the total concentration of bivalent ligand [L2]0, the total concentration of protein [P]0, one dissociation constant Kd, and a parameter to account for cooperativity alpha. We d ...[more]

PMID: 18543951

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