Resolving Three-State Ligand-Binding Mechanisms By Isothermal Titration Calorimetry: A Simulation Study

Authors

Evgueni Kovriguine, Marquette UniversityFollow

Document Type

Article

Language

English

Publication Date

6-2017

Publisher

Cold Spring Harbor Laboratory Press

Source Publication

bioRxiv beta

Abstract

In this paper, I theoretically analyzed ITC profiles for three-state equilibria involving ligand binding coupled to isomerization or dimerization transitions. Simulations demonstrate that the mechanisms where the free or ligand-bound protein undergoes dimerization (such that the ligand cannot bind to or dissociate from the dimer) produce very distinctive titration profiles. In contrast, profiles of the pre-existing equilibrium or induced-fit models cannot be distinguished from a simple two-state process, requiring data from additional techniques to positively identify these mechanisms.

Comments

Accepted version. bioRxiv beta (June 2017). DOI. 2017 Cold spring Harbor Laboratory Press. Used with permission.

Creative Commons License

This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.

Recommended Citation

Kovriguine, Evgueni, "Resolving Three-State Ligand-Binding Mechanisms By Isothermal Titration Calorimetry: A Simulation Study" (2017). Chemistry Faculty Research and Publications. 577.
https://epublications.marquette.edu/chem_fac/577